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2-aminopentanoate + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
-
activity with 2-oxovalerate amd 2-aminopentanoate is 25% and 17% compared to the activity with 2-oxoglutarate and L-glutamate
-
-
r
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
2-oxovalerate + NADPH + NH3
L-2-aminovalerate + NADP+ + H2O
-
15% of the activity with 2-oxoglutarate
-
-
?
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
L-2-oxoglutarate + NADPH + NH3
glutamate + NADP+ + H2O
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
L-homoserine + H2O + NAD+
4-hydroxy-2-oxobutanoate + NH3 + NADH
-
-
-
?
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
additional information
?
-
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
-
6.3% of the activity with 2-oxoglutarate
-
-
?
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
-
6.3% of the activity with 2-oxoglutarate
-
-
?
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
2.6% of the activity with 2-oxoglutarate
-
-
r
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
2.6% of the activity with 2-oxoglutarate
-
-
r
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
-
12% of the activity with 2-oxoglutarate
-
-
?
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
-
12% of the activity with 2-oxoglutarate
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
NH4Cl used in enzyme assay
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
weak activity
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
AKQ74236
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
AKQ74236
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
136% of the activtiy with L-glutamate
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
136% of the activtiy with L-glutamate
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
referred reaction
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
ir
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
Thermophilic bacillus
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
4.2% of the activity with 2-oxoglutarate
-
-
r
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
4.2% of the activity with 2-oxoglutarate
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
usage of NH4Cl as substrate for the reverse reaction
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
usage of NH4Cl as substrate for the reverse reaction
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination. No activity with the following amino acids in oxidative deamination: D-glutamate, L-norvaline, L-2-aminobutyrate, L-valine, L-alanine, L-aspartate, L-serine, L-cysteine, L-lysine, or L-phenylalanin. No activity with the following amino acids in reductive amination: pyruvate, 2-oxovalerate, 2-oxoisocaproate, 2-oxobutyrate, or 2-oxoisovalerate
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
AKQ74236
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
AKQ74236
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
reaction cycle, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia, biphasic kinetic behavior for L-glutamate
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
Thermophilic bacillus
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
biphasic kinetic behavior for ammonia
r
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
3% of the activity with L-glutamate
-
-
r
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
3% of the activity with L-glutamate
-
-
r
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
?
additional information
?
-
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
?
additional information
?
-
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
?
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
?
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
?
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
?
additional information
?
-
-
enzyme additionally shows activity towards hexanol and isoamyl alcohol
-
-
?
additional information
?
-
-
enzyme additionally shows activity towards hexanol and isoamyl alcohol
-
-
?
additional information
?
-
-
no activity with 2-oxoisovalerate and pyruvate
-
-
?
additional information
?
-
-
no activity with 2-oxoisovalerate and pyruvate
-
-
?
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
?
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
?
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
?
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
?
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
?
additional information
?
-
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
?
additional information
?
-
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
?
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
?
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
additional information
?
-
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
-
-
-
-
ir
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
Thermophilic bacillus
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
?
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
?
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
?
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
?
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
?
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
?
additional information
?
-
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
?
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
?
additional information
?
-
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
?
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
?
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
?
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2,4-pyridinedicarboxylate
2-hydroxyethyl disulfide
attenuation of reductive amination (forward) activity but a negligible effect on oxidative deamination (reverse) activity
Ag2+
-
at 1 mM, 60% inhibition
AgNO3
-
1 mM, 30°C, complete loss of aminating activity
BaCl2
-
1 mM, 30°C, 15% loss of aminating activity
benzene-1,3-dicarboxamide
-
-
bis(2,2,2-trifluoroethyl) benzene-1,3-dicarboxylate
-
-
CaCl2
-
1 mM, 30°C, 11% loss of aminating activity
CH2ICOOH
-
1 mM, 30°C, 15% loss of aminating activity
cystine
strongly and selectively inhibits the reductive amination reaction
dibenzyl benzene-1,3-dicarboxylate
-
-
dimethyl 4,4'-[1,3-phenylenebis(carbonylazanediyl)]di(cyclopent-2-ene-1-carboxylate)
-
-
dimethyl benzene-1,3-dicarboxylate
-
-
dimethyl ester of isophthalic acid
-
dimethyl ester of isophthalate (DMIP), but not isophthalate, inhibits Aspergillus niger growth on agar as well as in liquid culture. This is ascribed to the inability of isophthalate to enter fungal mycelia. Dimethyl ester of isophthalic acid is hydrolysed intracellularly to isophthalate. Subsequent to DMIP addition, intracellular isophthalate can be demonstrated. Addition of NH4+ to DMIP-treated Aspergillus niger mycelia results in intensive vacuolation, retraction of cytoplasm and autolysis
dipropan-2-yl benzene-1,3-dicarboxylate
-
-
dithiothreitol
-
1 mM, 30.7% residual activity
EDTA
-
1 mM, 5.3% residual activity
epigallocatechingallate
EGCG
-
FeSO3(NH4)2SO4
-
1 mM, 30°C, 14% loss of aminating activity
glutamate
-
competitive inhibitor of the amination reaction
Glutaric acid
-
at 20 mM, 25% inhibition
glyoxylate
-
at 20 mM, 30% inhibition
Hexachlorophene
15% inhibition at 0.016 mM; 80% inhibition at 0.016 mM
hydroxylamine
-
competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
iodoacetamide
-
at 4 mM, complete inactivation
isocitrate
10 M, 64% of initial activity
L-glutamate
-
substrate inhibition above 15 mM
L-Glutamic acid
-
at 20 mM 25% inhibition
L-homoserine
-
competitive inhibitor with respect to both ammonia and glutamine
L-tryptophan
-
at 20 mM, 15% inhibition
N-ethylmaleimide
-
at 0.8 mM, 44% inhibition
N1,N1,N3,N3-tetra(propan-2-yl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(2-amino-2-oxoethyl)isophthalamide
-
-
N1,N3-bis(2-chlorophenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(3,5-dichlorophenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(3-fluorophenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(3-hydroxyphenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(4-fluorophenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(4-methoxyphenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis(5-tert-butyl-2-hydroxyphenyl)benzene-1,3-dicarboxamide
-
-
N1,N3-bis[3,5-bis(trifluoromethyl)phenyl]benzene-1,3-dicarboxamide
-
-
N1,N3-bis[[3,5-bis(trifluoromethyl)phenyl]methyl]benzene-1,3-dicarboxamide
-
-
N1,N3-dihydroxybenzene-1,3-dicarboxamide
-
-
N1,N3-dimethoxybenzene-1,3-dicarboxamide
-
-
N1,N3-diphenylbenzene-1,3-dicarboxamide
-
-
NAD+
-
0.3 mM, 50.5% residual activity
NADH
-
0.3 mM, 5.3% residual activity
NADP+
-
inhibits at higher 2-oxoglutarate levels
NADPH
-
0.3 mM, 3.8% residual activity
nitrogen assimilation control protein
-
represses the transcription of the gene gdhA
-
p-chloromercuriphenyl sulfonate
-
inactivetes, can be reversed by addition of cysteine
p-hydroxymercuribenzoic acid
Pb2+
-
5 mM, 19.8% residual activity
potassium phosphate
-
over 0.1 M at oxidative deamination
propylselen
inhibits glutamate dehydrogenase by binding at the NADP+ binding site. No inhibition of enzyme mutant P320A
-
pyruvate
-
at 10 mM slight inhibitory
sodium dodecylsulfate
-
at 0.7% w/v after 1 h 5% activity
succinate
-
competitive inhibitor with 2 oxoglutarate, uncompetitive with NADPH and non-competitive with ammonia
2,4-pyridinedicarboxylate
-
-
2,4-pyridinedicarboxylate
-
inhibits less efficiently
2,4-pyridinedicarboxylate
-
weak inhibitor
2-Methyleneglutarate
-
-
2-Methyleneglutarate
-
weak inhibitor
2-oxoglutarate
-
shows allosteric properties and a sigmoid response (nH=2.5) towards 2-oxoglutarate saturation
2-oxoglutarate
-
substrate inhibition above 2.0 mM
2-oxoglutarate
-
competitive inhibitor of the deamination
4-chloromercuribenzoate
-
at 1 mM, 86% inhibition
4-chloromercuribenzoate
-
at 1 mM and 10 mM, 30% inhibition and 100% inhibition
4-chloromercuribenzoate
-
at 0.01 mM, 35% inhibition
ADP
-
at 4 mM slight inhibitory
ADP
-
at 0.3 mM, 22% inhibition of oxidative deamination
ADP
-
at 1 mM, 57% inhibition for oxidative deamination and 23% inhibition for reductive amination respectively
AlCl3
-
1 mM, 30°C, 23% loss of aminating activity
AlCl3
-
at 1 mM, 30% inhibition
AlCl3
-
at 1 mM, 21% inhibition
AMP
-
slight inhibitory
AMP
-
inhibitory at higher concentrations than 1 mM
AMP
-
at 0.3 mM 33% inhibition of oxidative deamination
ATP
-
at 4 mM slight inhibitory
ATP
-
1 mM, 14.4% residual activity
Ca2+
-
at 1 mM 27% inhibition
Ca2+
-
5 mM, 93.5% residual activity
fumarate
-
at 5 mM 20% inhibition
fumarate
-
at 20 mM 30% inhibition
guanidine hydrochloride
-
complete loss of activity
guanidine hydrochloride
-
complete loss of activity
Hg2+
-
at 1 mM, 70% inhibition
Hg2+
-
at 1 mM, 100% activity loss
Hg2+
-
at 1 mM, 10% inhibition
Hg2+
-
at 1 mM, 100% activity loss
Hg2+
1 mM, 76% residual activity
Hg2+
-
at 0.1 mM, complete activity loss
HgCl2
-
1 mM, 30°C, 48% loss of aminating activity
HgCl2
-
at 1 mM, 64% inhibition
HgCl2
-
at 1 mM, 45% inhibition
HgCl2
-
at 0.01 mM, 27% inhibition
HgCl2
-
at 1 mM, no activity, oxidative deamination
isophthalate
-
-
isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
isophthalate
-
potent in vitro inhibitor
isophthalate
-
weak inhibitor
isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
isophthalic acid
-
-
KCl
-
500 mM, 80-90% inhibition, by high ionic strength
KCl
100 mM, 45% residual activity
KCl
1 M, 30% loss of activity
malate
-
at 5 mM, 20% inhibition
malate
-
at 20 mM, 30% inhibition
Mg2+
-
at 1 mM, 16% activity loss
Mg2+
-
5 mM, 68% residual activity
Mn2+
-
at 1 mM, 19% activity loss
Mn2+
-
5 mM, 51.8% residual activity
MnCl2
-
at 1 mM, 63% inhibition
MnCl2
-
at 1 mM, 20% inhibition
NaCl
-
50 mM, 50% inhibition. 100 mM, about 60% inhibition. 500 mM, about 90% inhibition by high ionic strength
NaCl
100 mM, 59% residual activity
NH4+
-
-
NH4+
-
inhibits the oxidative deamination activity as a product, inhibition is non-competitive with respect to L-glutamate
oxaloacetate
-
at 20 mM slight inhibitory
oxaloacetate
-
at 20 mM, 60% inhibition
oxaloacetate
10 mM, 63% residual activity
p-hydroxymercuribenzoic acid
-
at 0.08 mM, 50% inhibition
p-hydroxymercuribenzoic acid
-
at 10 mM, 90% inhibition after 40 min
Pb(CH3COO)2
-
at 1 mM, 59% inhibition
Pb(CH3COO)2
-
at 1 mM, 64% inhibition
pyridoxal 5'-phosphate
-
at 10 mM, 90% inhibition, complete protection when 16.8 mM 2-oxoglutarate and 1.68 mM NADP+ are added
pyridoxal 5'-phosphate
-
at 1 mM, 35% inhibition
pyridoxal 5'-phosphate
-
at 1 mM, 45% inhibition
Urea
-
at 0°C 1 h at 2 M 65% inhibition
Urea
-
at 8 M stable for 10 min
Urea
-
no activity at 6 mM
Urea
-
inactivation with 2 mM urea
Urea
-
fully active at 20°C in 8 mM urea
Zn2+
-
at 1 mM, 64% activity loss
Zn2+
-
at 1 mM, 40% inhibition
additional information
-
not inhibited by D-glutamate, L-glutamine or DL-2-hydroxyglutarate
-
additional information
not inhibitory/activating: oxidized glutathione
-
additional information
-
not inhibitory/activating: oxidized glutathione
-
additional information
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
-
additional information
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
-
additional information
-
structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains; structural analogues of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives are designed, synthesized and screened for inhibition of NADP-GDH activity as well as YeH transition in Benjaminiella poitrasii, and also in human pathogenic Candida albicans strains, effect of dimethyl esters of isophthalate (DMIP) derivatives on Benjaminiella poitrasii yeast-hypha transition in vivo, overview. The dimethyl esters of isophthalic acid (DMIP) compounds show a more pronounced effect on H-form specific BpNADPGDH II and inhibit YeH transition as well as growth in Benjaminiella poitrasii and Candida albicans strains
-
additional information
-
2-oxoglutarate and NH3 show substrate inhibition
-
additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
-
additional information
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
-
additional information
-
no effect: EDTA, o-phenanthroline, sodium azide, 8-hydroxyquinoline in the concentration raneg of 1-10 mM
-
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0.004 - 606
2-oxoglutarate
0.0417 - 1349
L-glutamate
3.629
NAD+
-
pH 9.0, 50°C
additional information
additional information
-
0.004
2-oxoglutarate
-
pH not specified in the publication, 30°C
0.018
2-oxoglutarate
-
pH 8.5, 40°C
0.16
2-oxoglutarate
-
reductive amination at 80°C
0.2
2-oxoglutarate
-
reductive amination
0.2
2-oxoglutarate
pH 7.0, 25°C, recombinant enzyme
0.27
2-oxoglutarate
pH 8.0, 80°C
0.28
2-oxoglutarate
-
reductive amination
0.31
2-oxoglutarate
-
isoform Gdh1, pH 5.8, 30°C
0.32
2-oxoglutarate
-
reductive amination
0.34
2-oxoglutarate
-
reductive amination at 25°C
0.34
2-oxoglutarate
-
pH 5.8, 30°C
0.36
2-oxoglutarate
-
reductive amination
0.365
2-oxoglutarate
pH 7.0, 25°C, recombinant enzyme
0.37
2-oxoglutarate
-
isoform Gdh1, pH 7.5, 30°C
0.4
2-oxoglutarate
-
reductive amination
0.4
2-oxoglutarate
-
isoform Gdh3, pH 7.5, 30°C
0.46
2-oxoglutarate
-
pH 7.5, 30°C
0.5
2-oxoglutarate
-
reductive amination
0.5
2-oxoglutarate
-
reductive amination at 60°C
0.64
2-oxoglutarate
-
reductive amination
0.64
2-oxoglutarate
-
reductive amination
0.68
2-oxoglutarate
-
in the presence of 100 mM NH4Cl, at 25°C and pH 8
0.68
2-oxoglutarate
-
wild-type EcGDH, Vmax: 464 micromol/min/mg, pH 8.0, 25°C
0.77
2-oxoglutarate
-
reductive amination
0.89
2-oxoglutarate
wild-type, pH 7.0,30°C
0.93
2-oxoglutarate
-
reductive amination
1
2-oxoglutarate
-
reductive amination
1.1
2-oxoglutarate
-
in the presence of 200 mM NH4Cl, at 25°C and pH 8
1.2
2-oxoglutarate
-
reductive amination
1.25
2-oxoglutarate
-
reductive amination
1.3
2-oxoglutarate
Thermophilic bacillus
-
reductive amination
1.48
2-oxoglutarate
-
isoform Gdh3, S0.5 value, Hill coefficient 2.4, pH 5.8, 30°C
1.5
2-oxoglutarate
-
reductive amiantion
1.54
2-oxoglutarate
-
reductive amination
1.7
2-oxoglutarate
-
reductive amination at 50°C
1.7
2-oxoglutarate
-
reductive amination at 80°C
1.7
2-oxoglutarate
pH 9.0, 50°C
1.7
2-oxoglutarate
pH 8.3, 50°C
1.7
2-oxoglutarate
pH 9.5, 50°C, recombinant enzyme
1.95
2-oxoglutarate
-
S0.5 value, Hill coefficient 4, pH 5.8, 30°C
2
2-oxoglutarate
-
reductive amination at 0.6 M NH4Cl
2
2-oxoglutarate
-
reductive amination at 56°C
2.2
2-oxoglutarate
-
pH 8.0, 25°C
2.41
2-oxoglutarate
-
reductive amination
2.5 - 3
2-oxoglutarate
-
in the presence of 400 mM NH4Cl, at 25°C and pH 8
3
2-oxoglutarate
-
reductive amination at 25°C
3
2-oxoglutarate
-
reductive amination at 25°C
3.13
2-oxoglutarate
-
reductive amination at 30°C
3.2
2-oxoglutarate
-
reductive amination at 33°C
3.2
2-oxoglutarate
-
pH 7.0, 38.5°C, DELTA40N-homohexamer
3.25
2-oxoglutarate
-
reductive amination
3.61
2-oxoglutarate
-
S0.5 value, Hill coefficient 4.4, pH 7.5, 30°C
3.97
2-oxoglutarate
-
pH 8.0, 30°C, recombinant enzyme
4
2-oxoglutarate
-
reductive amination
4
2-oxoglutarate
mutant C141S, S0.5 value, Hill coefficient 2.3, pH 8.0, temperature not specified in the publication
4.73
2-oxoglutarate
AKQ74236
25°C, pH 7.5
4.78
2-oxoglutarate
-
28°C
4.78
2-oxoglutarate
wild-type, S0.5 value, Hill coefficient 3.2, pH 8.0, temperature not specified in the publication
5
2-oxoglutarate
-
reductive amination
5
2-oxoglutarate
-
pH 7.0, 38.5°C, alpha-homohexamer
5.6
2-oxoglutarate
-
reductive amination
5.7
2-oxoglutarate
recombinant wild-type, S0.5 value, Hill coefficient 3.5, pH 8.0, temperature not specified in the publication
6
2-oxoglutarate
-
pH 7.6, 60°C
6.8
2-oxoglutarate
-
pH 7.0, 38.5°C, beta-homohexamer
9
2-oxoglutarate
-
reductive amination at 1 M NH4Cl
15.5
2-oxoglutarate
mutant C415S, S0.5 value, Hill coefficient 4.9, pH 8.0, temperature not specified in the publication
25.1
2-oxoglutarate
wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 2.4, pH 8.0, temperature not specified in the publication
285
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25°C
606
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25°C
0.0417
L-glutamate
-
pH not specified in the publication, 30°C
0.22
L-glutamate
-
oxidative deamination at 80°C
0.24
L-glutamate
pH 8.0, 22°C, recombinant mutant K341L
0.45
L-glutamate
pH 8.0, 22°C, recombinant wild-type enzyme
0.6
L-glutamate
-
pH 7.6, 60°C
0.6
L-glutamate
pH 8.0, 22°C, recombinant mutant C321A
0.61
L-glutamate
pH 8.0, 25°C, recombinant enzyme
0.9
L-glutamate
pH 8.0, 22°C, recombinant mutant P320A
1.05
L-glutamate
pH 8.0, 25°C, recombinant enzyme
1.1
L-glutamate
Thermophilic bacillus
-
oxidative deamination
1.3
L-glutamate
-
oxidative deamination
1.3
L-glutamate
pH 8.0, 80°C
2
L-glutamate
-
reductive amination
2.2
L-glutamate
-
oxidative deamination
2.3
L-glutamate
-
oxidative deamination
2.3
L-glutamate
-
oxidative deamination
2.3
L-glutamate
-
at 25°C and pH 8
2.3
L-glutamate
-
wild-type EcGDH, Vmax: 37.9 micromol/min/mg, pH 8.0, 25°C
3.2
L-glutamate
-
oxidative deamination at 25°C
3.3
L-glutamate
-
oxidative deamination at 50°C
3.3
L-glutamate
pH 8.3, 50°C
3.4
L-glutamate
pH 10.5, 50°C, recombinant enzyme
3.4
L-glutamate
pH 9.5, 50°C
3.7
L-glutamate
-
reductive amination
3.9
L-glutamate
-
oxidative deamination at 60°C
5.18
L-glutamate
-
oxidative deamination
5.5
L-glutamate
-
oxidative deamination
6.06
L-glutamate
-
oxidative deamination at 30°C
6.36
L-glutamate
-
oxidative deamination, Gdh3p gene
9.12
L-glutamate
-
oxidative deamination at 80°C
9.79
L-glutamate
-
oxidative deamination, Gdh1p gene
10
L-glutamate
-
oxidative deamination
14.2
L-glutamate
-
oxidative deamination
15.15
L-glutamate
-
pH 8.0, 30°C, recombinant enzyme
18
L-glutamate
-
oxidative deamination, biphasic kinetics
21
L-glutamate
-
pH 7.0, 38.5°C, beta-homohexamer
23.29
L-glutamate
AKQ74236
25°C, pH 7.5
25
L-glutamate
-
pH 7.0, 38.5°C, DELTA40N-homohexamer
27
L-glutamate
-
oxidative deamination at 33°C
28.6
L-glutamate
-
oxidative deamination
28.6
L-glutamate
mutant C141S, pH 9.3, temperature not specified in the publication
29
L-glutamate
-
oxidative deamination
30.9
L-glutamate
recombinant wild-type, pH 9.3, temperature not specified in the publication
32.3
L-glutamate
-
oxidative deamination
34
L-glutamate
-
pH 7.0, 38.5°C, alpha-homohexamer
34.6
L-glutamate
wild-type, pH 9.3, temperature not specified in the publication
36.8
L-glutamate
mutant C415S, pH 9.3, temperature not specified in the publication
38.2
L-glutamate
-
oxidative deamination
44
L-glutamate
-
oxidative deamination
49.8
L-glutamate
wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 1.9, pH 9.3, temperature not specified in the publication
50
L-glutamate
wild-type, pH 7.0,30°C
67.4
L-glutamate
-
oxidative deamination
79
L-glutamate
-
oxidative deamination
81
L-glutamate
-
oxidative deamination, biphasic kinetics
225
L-glutamate
-
oxidative deamination
1349
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C
0.16
NADH
wild-type, pH 7.0,30°C
0.368
NADH
-
pH 9.0, 50°C
0.69
NADH
mutant K136A, pH 7.0,30°C
0.00007
NADP+
-
pH not specified in the publication, 30°C
0.0064
NADP+
-
oxidative deamination
0.0098
NADP+
-
recombinant enzyme, oxidative deamination
0.01
NADP+
-
oxidative deamination at 25°C
0.0102
NADP+
-
wild-type enzyme, oxidative deamination
0.0105
NADP+
-
oxidative deamination, Gdh3p gene
0.013
NADP+
-
oxidative deamination
0.013
NADP+
-
oxidative deamination
0.0141
NADP+
-
oxidative deamination, Gdh1p gene
0.015
NADP+
-
pH 7.0, 38.5°C, DELTA40N-homohexamer
0.017
NADP+
wild-type, pH 9.3, temperature not specified in the publication
0.018
NADP+
-
wild-type EcGDH, Vmax: 45.6 micromol/min/mg, pH 8.0, 25°C
0.0184
NADP+
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.019
NADP+
pH 8.0, 25°C, recombinant enzyme
0.02
NADP+
-
pH 7.6, 60°C
0.02
NADP+
pH 8.0, 25°C, recombinant enzyme
0.022
NADP+
wild-type inactivated by 2-hydroxyethyl disulfide, pH 9.3, temperature not specified in the publication
0.023
NADP+
-
oxidative deamination
0.027
NADP+
-
pH 7.0, 38.5°C, alpha-homohexamer
0.028
NADP+
-
pH 7.0, 38.5°C, beta-homohexamer
0.028
NADP+
recombinant wild-type, pH 9.3, temperature not specified in the publication
0.029
NADP+
-
oxidative deamination at 80°C
0.029
NADP+
-
oxidative deamination at 30°C
0.03
NADP+
-
oxidative deamination
0.031
NADP+
-
oxidative deamination
0.0328
NADP+
mutant K289Q, pH 8.0, temperature not specified in the publication
0.035
NADP+
pH 10.5, 50°C, recombinant enzyme
0.038
NADP+
-
oxidative deamination at 80°C
0.039
NADP+
-
oxidative deamination
0.039
NADP+
-
oxidative deamination at 50°C
0.04
NADP+
-
oxidative deamination
0.04
NADP+
-
oxidative deamination
0.041
NADP+
-
pH 8.0, 30°C, recombinant enzyme
0.042
NADP+
-
oxidative deamination
0.043
NADP+
-
oxidative deamination
0.043
NADP+
-
oxidative deamination
0.044
NADP+
-
oxidative deamination
0.045
NADP+
-
oxidative deamination
0.05
NADP+
-
oxidative deamination
0.053
NADP+
-
oxidative deamination
0.06
NADP+
-
oxidative deamination at 60°C
0.061
NADP+
-
oxidative deamination
0.07
NADP+
pH 8.0, 22°C, recombinant wild-type enzyme
0.0819
NADP+
mutant K292Q, pH 8.0, temperature not specified in the publication
0.088
NADP+
-
pH 9.0, 50°C
0.093
NADP+
wild-type, pH 7.0,30°C
0.1 - 1
NADP+
pH 8.0, 80°C
0.11
NADP+
-
oxidative deamination
0.117
NADP+
-
oxidative deamination at 33°C
0.12
NADP+
-
oxidative deamination
0.12
NADP+
-
oxidative deamination
0.129
NADP+
mutant K286Q, pH 8.0, temperature not specified in the publication
0.13
NADP+
pH 8.0, 22°C, recombinant mutant K341L
0.15
NADP+
pH 8.0, 22°C, recombinant mutant C321A
0.163
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C
0.3
NADP+
Thermophilic bacillus
-
oxidative deamination
0.3
NADP+
pH 8.0, 22°C, recombinant mutant P320A
0.929
NADP+
mutant K286Q/R289Q/R292Q , pH 8.0, temperature not specified in the publication
18.3
NADP+
mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication
18.4
NADP+
-
at 25°C and pH 8
19.06
NADP+
mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication
0.00013
NADPH
-
pH not specified in the publication, 30°C
0.003
NADPH
-
reductive amination
0.004
NADPH
-
reductive amination
0.007
NADPH
pH 7.0, 25°C, recombinant enzyme
0.0087
NADPH
-
reductive amination
0.0097
NADPH
-
reductive amination
0.01
NADPH
-
reductive amination
0.011
NADPH
wild-type, pH 8.0, temperature not specified in the publication
0.0113
NADPH
-
reductive amination, Gdh1p gene
0.012
NADPH
-
pH 7.6, 60°C
0.012
NADPH
pH 7.0, 25°C, recombinant enzyme
0.016
NADPH
wild-type, pH 7.0,30°C
0.017
NADPH
-
reductive amination
0.017
NADPH
pH 9.5, 50°C, recombinant enzyme
0.018
NADPH
-
reductive amination at 25°C
0.019
NADPH
-
reductive amination
0.02
NADPH
-
reductive amination
0.02
NADPH
-
reductive amination at 60°C
0.021
NADPH
-
pH 8.0, 25°C
0.022
NADPH
-
reductive amination at 50°C
0.023
NADPH
recombinant wild-type, pH 8.0, temperature not specified in the publication
0.024
NADPH
-
reductive amination
0.027
NADPH
-
reductive amination
0.027
NADPH
-
reductive amination
0.028
NADPH
-
reductive amination
0.03
NADPH
-
reductive amination at 25°C
0.0331
NADPH
-
reductive amination, Gdh3p gene
0.035
NADPH
-
reductive amination
0.039
NADPH
-
S0.5 value, Hill coefficient 1.8, pH 7.5, 30°C
0.04
NADPH
-
reductive amination
0.042
NADPH
-
isoform Gdh3, pH 7.5, 30°C
0.044
NADPH
-
reductive amination at 30°C
0.044
NADPH
wild-type inactivated by 2-hydroxyethyl disulfide, pH 8.0, temperature not specified in the publication
0.045
NADPH
-
isoform Gdh1, pH 7.5, 30°C
0.046
NADPH
-
pH 7.5, 30°C
0.049
NADPH
-
reductive amination
0.049
NADPH
-
reductive amination
0.053
NADPH
Thermophilic bacillus
-
reductive amination
0.058
NADPH
mutant K1376A, pH 7.0,30°C
0.06
NADPH
-
wild-type EcGDH, Vmax: 503 micromol/min/mg, pH 8.0, 25°C
0.064
NADPH
-
reductive amination
0.066
NADPH
-
reductive amination at 80°C
0.07
NADPH
-
reductive amination
0.073
NADPH
mutant R290A, pH 7.0,30°C
0.074
NADPH
-
reductive amination at 33°C
0.075
NADPH
-
reductive amination at 70°C
0.078
NADPH
-
reductive amination
0.083
NADPH
-
reductive amination
0.095
NADPH
-
reductive amination
0.11
NADPH
-
reductive amination
0.111
NADPH
AKQ74236
25°C, pH 7.5
0.125
NADPH
-
pH 7.0, 38.5°C, DELTA40N-homohexamer
0.14
NADPH
-
reductive amination at 80°C
0.14
NADPH
-
pH 7.0, 38.5°C, alpha-homohexamer
0.16
NADPH
mutant S265A, pH 7.0,30°C
0.26
NADPH
-
pH 7.0, 38.5°C, beta-homohexamer
0.28
NADPH
-
pH 9.0, 50°C
0.34
NADPH
-
pH 8.0, 30°C, recombinant enzyme
0.51
NADPH
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25°C
59.7
NADPH
-
at 25°C and pH 8
0.00056
NH3
-
recombinant enzyme, reductive amination
0.00065
NH3
-
wild-type enzyme, reductive amination
1.05
NH3
wild-type, pH 8.0, temperature not specified in the publication
1.1
NH3
recombinant wild-type, pH 8.0, temperature not specified in the publication
1.16
NH3
-
pH 8.0, 30°C, recombinant enzyme
1.2
NH3
mutant C141S, pH 8.0, temperature not specified in the publication
1.48
NH3
-
pH 8.0, 25°C, recombinant enzyme
1.89
NH3
-
in the presence of 20 mM 2-oxoglutarate, at 25°C and pH 8
2.2
NH3
pH 9.5, 50°C, recombinant enzyme
2.47
NH3
-
in the presence of 5 mM 2-oxoglutarate, at 25°C and pH 8
2.5
NH3
-
reductive amination
2.5 - 3
NH3
-
in the presence of 2.5 mM 2-oxoglutarate, at 25°C and pH 8
2.6
NH3
wild-type inactivated by 2-hydroxyethyl disulfide, pH 8.0, temperature not specified in the publication
4
NH3
-
reductive amination
4
NH3
-
reductive amination at 60°C
4.56
NH3
-
reductive amination
5
NH3
-
reductive amination, Gdh3p gene
5.96
NH3
-
reductive amination, Gdh1p gene
5.96
NH3
-
reductive amination at 30°C
6.9
NH3
-
isoform Gdh3, pH 7.5, 30°C
8.6
NH3
-
isoform Gdh1, pH 7.5, 30°C
21.4
NH3
-
S0.5 value, Hill coefficient 2.7, pH 7.5, 30°C
33
NH3
wild-type, pH 7.0,30°C
119
NH3
-
reductive amination at 70°C
0.29
NH4+
-
reductive amination
0.37
NH4+
-
reductive amination
0.63
NH4+
-
reductive amination at 80°C
1.1
NH4+
-
reductive amination
1.7
NH4+
-
reductive amination
2
NH4+
-
reductive amination
2.1
NH4+
-
reductive amination at 33°C
2.2
NH4+
-
reductive amination
2.2
NH4+
-
reductive amination at 25°C
2.5 - 3
NH4+
-
wild-type EcGDH, Vmax: 298 micromol/min/mg, pH 8.0, 25°C
2.6
NH4+
-
reductive amination, biphasic kinetics
3.3
NH4+
-
reductive amination alpha-isoenzyme, depending on NADPH-concentration
3.7
NH4+
-
reductive amination
4.2
NH4+
-
reductive amination at 25°C
6.5
NH4+
-
reductive amination
6.6
NH4+
-
pH 7.0, 38.5°C, alpha-homohexamer
6.76
NH4+
-
reductive amination
7.5
NH4+
-
reductive amination at 56°C
7.7
NH4+
-
reductive amination
9
NH4+
-
reductive amination
9.2
NH4+
-
reductive amination
10
NH4+
-
reductive amination
10.8
NH4+
-
pH 7.0, 38.5°C, DELTA40N-homohexamer
15.5
NH4+
-
reductive amination at 80°C
16.6
NH4+
-
reductive amination
20
NH4+
-
reductive amination
21
NH4+
Thermophilic bacillus
-
reductive amination
21.2
NH4+
-
reductive amination
21.2
NH4+
-
biphasic kinetics
22
NH4+
-
reductive amination
30.8
NH4+
-
reductive amination
36
NH4+
-
reductive amination
66
NH4+
-
reductive amination
75
NH4+
-
reductive amination beta-isoenzyme
80
NH4+
-
pH 7.0, 38.5°C, beta-homohexamer
83
NH4+
-
reductive amination at 50°C
304
NH4+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C
416
NH4+
-
reductive amination
additional information
additional information
-
kinetic analysis, overview, the isozyme GDHI' shows negative cooperativity with NH4+ substrate, with a decreased affinity for NH4Cl
-
additional information
additional information
-
kinetic analysis, overview, the isozymes show negative cooperativity with NH4+ substrate, with a decreased affinity for NH4Cl
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
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0.0015 - 0.0023
bis(2,2,2-trifluoroethyl) benzene-1,3-dicarboxylate
-
0.0035 - 0.0043
dimethyl 4,4'-[1,3-phenylenebis(carbonylazanediyl)]di(cyclopent-2-ene-1-carboxylate)
-
0.0122 - 0.0125
dimethyl benzene-1,3-dicarboxylate
-
0.00026 - 0.00274
ebselen
0.000202 - 0.000333
epigallocatechingallate
-
0.0053 - 0.0058
N1,N3-bis(2-amino-2-oxoethyl)isophthalamide
-
0.0032 - 0.0035
N1,N3-bis(2-chlorophenyl)benzene-1,3-dicarboxamide
-
0.0043 - 0.0061
N1,N3-bis(3,5-dichlorophenyl)benzene-1,3-dicarboxamide
-
0.0035 - 0.0039
N1,N3-bis(3-fluorophenyl)benzene-1,3-dicarboxamide
-
0.0073 - 0.0081
N1,N3-bis(3-hydroxyphenyl)benzene-1,3-dicarboxamide
-
0.0021 - 0.0026
N1,N3-bis(4-fluorophenyl)benzene-1,3-dicarboxamide
-
0.0068 - 0.007
N1,N3-bis(4-methoxyphenyl)benzene-1,3-dicarboxamide
-
0.0062 - 0.0073
N1,N3-bis(5-tert-butyl-2-hydroxyphenyl)benzene-1,3-dicarboxamide
-
0.0059 - 0.0062
N1,N3-bis[3,5-bis(trifluoromethyl)phenyl]benzene-1,3-dicarboxamide
-
0.0018 - 0.0029
N1,N3-bis[[3,5-bis(trifluoromethyl)phenyl]methyl]benzene-1,3-dicarboxamide
-
0.0049 - 0.0051
N1,N3-dihydroxybenzene-1,3-dicarboxamide
-
0.0037 - 0.0038
N1,N3-dimethoxybenzene-1,3-dicarboxamide
-
0.000469 - 0.00189
propylselen
-
additional information
additional information
-
0.0015
bis(2,2,2-trifluoroethyl) benzene-1,3-dicarboxylate
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0023
bis(2,2,2-trifluoroethyl) benzene-1,3-dicarboxylate
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0252
bithionol
Plasmodium falciparum
pH 8.0, 25°C, recombinant enzyme
0.12
bithionol
Plasmodium falciparum
pH 8.0, 25°C, recombinant enzyme
0.0035
dimethyl 4,4'-[1,3-phenylenebis(carbonylazanediyl)]di(cyclopent-2-ene-1-carboxylate)
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0043
dimethyl 4,4'-[1,3-phenylenebis(carbonylazanediyl)]di(cyclopent-2-ene-1-carboxylate)
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0122
dimethyl benzene-1,3-dicarboxylate
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0125
dimethyl benzene-1,3-dicarboxylate
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.00026
ebselen
Escherichia coli
pH 8.0, 22°C, recombinant mutant K341L, 2.5 mm Glu
0.0005
ebselen
Escherichia coli
pH 8.0, 22°C, recombinant wild-type enzyme, 2.5 mm Glu
0.0016
ebselen
Escherichia coli
pH 8.0, 22°C, recombinant mutant C321A, 2.5 mm Glu
0.00274
ebselen
Escherichia coli
pH 8.0, 22°C, recombinant mutant P320A, 2.5 mm Glu
0.000202
epigallocatechingallate
Escherichia coli
pH 8.0, 22°C, recombinant mutant C321A, 2.5 mm Glu
-
0.000202
epigallocatechingallate
Escherichia coli
pH 8.0, 22°C, recombinant mutant P320A, 2.5 mm Glu
-
0.000204
epigallocatechingallate
Escherichia coli
pH 8.0, 22°C, recombinant wild-type enzyme, at 2.5 mm Glu
-
0.000333
epigallocatechingallate
Escherichia coli
pH 8.0, 22°C, recombinant mutant K341L, 2.5 mm Glu
-
0.139
GW5074
Plasmodium falciparum
pH 8.0, 25°C, recombinant enzyme
0.15
GW5074
Plasmodium falciparum
pH 8.0, 25°C, recombinant enzyme
0.0053
N1,N3-bis(2-amino-2-oxoethyl)isophthalamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0058
N1,N3-bis(2-amino-2-oxoethyl)isophthalamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0032
N1,N3-bis(2-chlorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0035
N1,N3-bis(2-chlorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0043
N1,N3-bis(3,5-dichlorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0061
N1,N3-bis(3,5-dichlorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0035
N1,N3-bis(3-fluorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0039
N1,N3-bis(3-fluorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0073
N1,N3-bis(3-hydroxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0081
N1,N3-bis(3-hydroxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0021
N1,N3-bis(4-fluorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0026
N1,N3-bis(4-fluorophenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0068
N1,N3-bis(4-methoxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.007
N1,N3-bis(4-methoxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0062
N1,N3-bis(5-tert-butyl-2-hydroxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0073
N1,N3-bis(5-tert-butyl-2-hydroxyphenyl)benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0059
N1,N3-bis[3,5-bis(trifluoromethyl)phenyl]benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0062
N1,N3-bis[3,5-bis(trifluoromethyl)phenyl]benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0018
N1,N3-bis[[3,5-bis(trifluoromethyl)phenyl]methyl]benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0029
N1,N3-bis[[3,5-bis(trifluoromethyl)phenyl]methyl]benzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0049
N1,N3-dihydroxybenzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.0051
N1,N3-dihydroxybenzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0037
N1,N3-dimethoxybenzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH II, pH 8.0, 22°C
-
0.0038
N1,N3-dimethoxybenzene-1,3-dicarboxamide
Benjaminiella poitrasii
recombinant isozyme BpNADPGDH I, pH 8.0, 22°C
-
0.000469
propylselen
Escherichia coli
pH 8.0, 22°C, recombinant wild-type enzyme, 2.5 mm Glu
-
0.000585
propylselen
Escherichia coli
pH 8.0, 22°C, recombinant mutant K341L, 2.5 mm Glu
-
0.00189
propylselen
Escherichia coli
pH 8.0, 22°C, recombinant mutant C321A, 2.5 mm Glu
-
additional information
additional information
Benjaminiella poitrasii
IC50 values in microg/ml, cytotoxic MIC90 and IC50 values, overview
-
additional information
additional information
Benjaminiella poitrasii
IC50 values in microg/ml, cytotoxic MIC90 and IC50 values, overview
-
additional information
additional information
Benjaminiella poitrasii
-
IC50 values in microg/ml, cytotoxic MIC90 and IC50 values, overview
-
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evolution
altered localization to the mitochondria or peroxisomes prevents Gdh1, which was originally localized in the cytoplasm, from stationary phase-specific aggregation, suggesting that some cytosolic factors are involved in the process of Gdh1 aggregation
evolution
the BpNADPGDH I and II sequences from Benjaminiella poitrasii include the three typical motifs of the family I hexameric GDHs: 84 PSVNL88, 92KFLGFEQ98 and 184RPEATGY/F 190. One of the conserved regions in the sequences includes the putative NADP-binding motif GSGNVAQYAALKVIELG, located between the residues 219 and 235. BpNADPGDH I and BpNADPGDH II share 70% homology with each other, and BpNADPGDH I and BpNADPGDH II give over 70% identity scores with fungal NADP-dependent GDHs
evolution
-
altered localization to the mitochondria or peroxisomes prevents Gdh1, which was originally localized in the cytoplasm, from stationary phase-specific aggregation, suggesting that some cytosolic factors are involved in the process of Gdh1 aggregation
-
malfunction
-
two industrial strains of Penicillium chrysogenum a penicillin (PC-pen)- and a cephalosporin producing (PC-ceph) are used in which the NADPH-dependent GDH is deleted by replacing 0.8 kb of the C-terminus of the gdhA gene with the hygromyin B resistance marker, resulting in PC-pen-DELTAgdhA and PC-ceph-DELTAgdhA. The two strains are isogenic except for the insertion of the Streptomyces clavuligerus expandase gene into the genome of PC-ceph. It is shown that this genetic modification results in a radical change in morphology
malfunction
-
Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
malfunction
contradictory roles of GDH1 and GDH2 (EC 1.4.1.2) in cold-growth defects in yeast strains. Concurrent ectopic overexpression of GDH1 and GDH2 compensate the observed accumulation of ROS. Specifically, glutamate can prevent cold-induced ROS accumulation through the synthesis of glutathione that requires glutamate as a precursor molecule and serves in ROS removal. The role of Gdh1p in transcriptional silencing is crucial through the proteolysis of H3 histone in yeast (H3-clipping in the N-tail). GDH1 deletion leads to decreased binding of Sir2 protein on the telomeres, causing elevated transcript levels of genes affected by the loss of the SIR complex. Upon GDH1 deletion, the elevated levels of 2-oxoglutarate, and not those of NADH, result in the observed telomeric silencing defects. Upon GDH1 deletion, a highly derepressed expression of DAL5, a NCR-sensitive gene that requires both Gat1 and Gln3 for its expression, is observed. GDH1 deletion causes ammonium accumulation, but surprisingly does not affect the subcellular distribution and the concentrations of glutamine as well as glutamate
malfunction
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
malfunction
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
malfunction
propylselen inhibits cancer cell growth by targeting glutamate dehydrogenase at the NADP+ binding site
malfunction
-
Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
-
malfunction
-
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
-
malfunction
-
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
-
malfunction
-
contradictory roles of GDH1 and GDH2 (EC 1.4.1.2) in cold-growth defects in yeast strains. Concurrent ectopic overexpression of GDH1 and GDH2 compensate the observed accumulation of ROS. Specifically, glutamate can prevent cold-induced ROS accumulation through the synthesis of glutathione that requires glutamate as a precursor molecule and serves in ROS removal. The role of Gdh1p in transcriptional silencing is crucial through the proteolysis of H3 histone in yeast (H3-clipping in the N-tail). GDH1 deletion leads to decreased binding of Sir2 protein on the telomeres, causing elevated transcript levels of genes affected by the loss of the SIR complex. Upon GDH1 deletion, the elevated levels of 2-oxoglutarate, and not those of NADH, result in the observed telomeric silencing defects. Upon GDH1 deletion, a highly derepressed expression of DAL5, a NCR-sensitive gene that requires both Gat1 and Gln3 for its expression, is observed. GDH1 deletion causes ammonium accumulation, but surprisingly does not affect the subcellular distribution and the concentrations of glutamine as well as glutamate
-
metabolism
NADP+-GDH is involved in nitrogen assimilation due to a constitutive aminating activity, specific activity of the aminating NADP+-GDH reaction is independent of nitrogen availability, it does not change significantly in response to prolonged exposure to nitrogen limitation, in contrast to the deaminating activity, which is 2fold increased exposed to ammonium starvation conditions. The deaminating reaction changes in response to varying ammonium concentrations and is regulated in response to nitrogen availability. NADP+-GDH is not regulated on the transcriptional level. The enzyme is invovled in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH, regulation of NADP+-GDH specific activity, overview
metabolism
-
both NADP(H)-GDH (gdhA) and glutamine synthetase play important roles in ammonium assimilation
metabolism
in Saccharomyces cerevisiae glutamate can be synthesized from 2-oxoglutarate and ammonium through the action of NADP-dependent glutamate dehydrogenase isozymes Gdh1 and Gdh3. Gdh1 and Gdh3 are evolutionarily adapted isoforms and cover the anabolic role of the GDH-pathway, role and function of the GDH pathway in glutamate metabolism, overview. The pleiotropic effects of GDH pathway in yeast biology highlight the importance of glutamate homeostasis in vital cellular processes. Isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The constant expression of GDH1 implies that its transcription proceeds normally during the different growth phases including the diauxic shift, when yeast cells reprogram their metabolism to enter the respiration phase. But during the post-diauxic shift, the Gdh1p/Gdh3p ratio decreases and most of the NADP-GDH activity is attributed to Gdh3p. The decrease of the NADP-GDH activity in ethanol growing cells was initially referred to be controlled through post-translational modifications that can modulate the proportion of Gdh1p versus Gdh3p monomers that constitute the NADP-GDH pool. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes). NAD-GDH activity (encoded by GDH2, EC 1.4.1.2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate
metabolism
-
the enzyme is involved in the ammonium assimilation mechanism in submerged macrophytes, ammonium detoxification mechanism in ammonium-tolerant species, overview
metabolism
-
the enzyme is involved in the ammonium assimilation mechanism in submerged macrophytes, ammonium detoxification mechanism in ammonium-tolerant species, overview
metabolism
YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
metabolism
-
YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
-
metabolism
-
in Saccharomyces cerevisiae glutamate can be synthesized from 2-oxoglutarate and ammonium through the action of NADP-dependent glutamate dehydrogenase isozymes Gdh1 and Gdh3. Gdh1 and Gdh3 are evolutionarily adapted isoforms and cover the anabolic role of the GDH-pathway, role and function of the GDH pathway in glutamate metabolism, overview. The pleiotropic effects of GDH pathway in yeast biology highlight the importance of glutamate homeostasis in vital cellular processes. Isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The constant expression of GDH1 implies that its transcription proceeds normally during the different growth phases including the diauxic shift, when yeast cells reprogram their metabolism to enter the respiration phase. But during the post-diauxic shift, the Gdh1p/Gdh3p ratio decreases and most of the NADP-GDH activity is attributed to Gdh3p. The decrease of the NADP-GDH activity in ethanol growing cells was initially referred to be controlled through post-translational modifications that can modulate the proportion of Gdh1p versus Gdh3p monomers that constitute the NADP-GDH pool. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes). NAD-GDH activity (encoded by GDH2, EC 1.4.1.2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate
-
metabolism
-
YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
-
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: GDHI from isophthalate- and mHB-grown cells retain 70% and 90% of its activity, respectively
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: In Pseudomonas aeruginosa strain PPD, isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH, while PPD cells grown on pHB and benzoate show 25% and 40% loss of activity
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60°C are analysed: isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH
physiological function
-
to test the effect of decreased hGDH expression, small interfering hGDH RNAs are expressed intracellularly in BE(2)C human neuroblastoma cells. hGDH mRNA knockdown is confirmed by immunoblotting and RT-PCR. TUNEL and DNA fragmentation assays 48 h after transfection reveal that inhibition of hGDH expression induces cellular apoptosis and activates phospho-ERK1/2 (phospho-extracellular-signal-regulated kinase 1/2)
physiological function
-
Gdh1p is the primary GDH enzyme and Gdh3p plays an evident role during aerobic glutamate metabolism
physiological function
-
involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
physiological function
a high-copy number of the GDH2-encoded NADH-specific glutamate dehydrogenase gene stimulates growth at 15°C, while overexpression of NADPH-specific GDH1 has detrimental effects. Cells overexpressing GDH1 still display a cold-sensitive phenotype in presence of tryptophan or nictotinic acid in the medium. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae
physiological function
-
expression in Oryza sativa. At the seedling stage, the leaf area and shoot and root dry weights of the high gdhA-expressors are higher than those of control plants under both high (high N) and low nitrogen (low N) conditions. The net photosynthesis rate at the heading stage is higher in transgenic than in control leaves. Under both high and low N conditions, the nitrogen contents in the shoots and roots, at seedling and grain-harvest stages, are significantly higher in high gdhA-expressors than in control plants. At the harvest stage, the high gdhA-expressors exhibit greater panicle and spikelet numbers per plant compared with control plants, resulting in higher grain weight. In addition, gdhA expression in forage rice significantly enhances their tolerance to salt stress compared to control plants
physiological function
AKQ74236
the rocG gene deletion mutant produces intracellular glutamic acid with a concentration of 90 ng/log (CFU), which is only 23.7% that of the wild-type. The poly-gamma.glutamic acid yield of the mutant is 5.37 g/l, a decrease of 45.3% compared to the wild type
physiological function
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM) dependent protein kinases, respectively
physiological function
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM)-dependent protein kinases, respectively
physiological function
gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
physiological function
glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
physiological function
-
in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent (EC 1.4.1.2) and NADPH-dependent GDH show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
-
in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent (EC 1.4.1.2) and NADPH-dependent GDH show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. GDH2 (EC 1.4.1.2) genetically interacts with GDH3 and controls stress-induced apoptosis. The transcription of GDH3 occurs extensively during the stationary phase. The activity of Gdh3p presents a 20 to 140fold increment when cells are grown under aerobic conditions. Under these conditions the majority of the total NADP-GDH activity is attributed to Gdh3p monomers that can contribute up to 70% to the pool, especially when cells enter or remain in aerobic metabolism for several days. Under acetate/raffinose conditions with ammonia as the only nitrogen source, yeast cells lacking GDH3 gene has a significant impairment in glutamate synthesis. The increase of the NADP-dependent GDH activity observed in gdh1DELTA mutants is presumably due to Gdh3p that seems to play a prominent role in glutamate metabolism under aerobic conditions. Glutamate synthesis under aerobic conditions is insufficient and requires additionally the activity of Gdh1p. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The glucose-repressed expression of GDH3 is attributed to the condensed chromatin organization of its promoter
physiological function
isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. Role of GDH1 and GDH2 (EC 1.4.1.2) in glutamate synthesis and its possible implication to oxidation stress defense through the glutathione system. GDH1 regulates chromatin through its catalytic activity. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The regulation of GDH1 under glucose conditions is performed by nitrogen catabolite repressor (NCR)-sensitive activators, Leu3p and activators exclusive for respiratory growth such as the HAP complex that coordinates nuclear and mitochondrial gene expression. Under ethanol conditions, GDH1 derepression is mediated by the Gcn4 and Hap4 transcriptional activators and is amplified by Gln3
physiological function
NADP-GDH isozyme Gdh3, but not Gdh1, mainly contributes to the oxidative stress resistance of stationary-phase cells. The insignificance of Gdh1 to stress resistance possibly results from conditional and reversible aggregation of Gdh1 into punctuate foci initiated in parallel with postdiauxic growth
physiological function
-
the activity of glutamate dehydrogenase in the ammonium-tolerant species Myriophyllum spicatum leaves increases 169% for NADH-dependent GDH and 103% for NADPH-dependent GDH with the [NH4+-N] increasing from 0 to 100 mg/l, performing a dose-response curve while glutamine synthetase activity slightly changes
physiological function
the gdh3/gdh3 mutant is able to grow on either arginine or proline as a sole carbon and nitrogen source, but the strain is locked in the yeast morphology in proline-containing medium. In proline medium, the gdh3/gdh3 mutant strain fails to form filaments, whilst the wild-type develops hyphae. Different concentrations of ATP, NAD+, NADH, NAPD+, NADPH, as well as 62 other metabolites, and 19 isotopically labelled are found metabolites between the mutant and the wild-type strains
physiological function
-
involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
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physiological function
-
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM)-dependent protein kinases, respectively
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physiological function
-
besides the distinct kinetic properties, the two isozymes in Benjaminiella poitrasii, BpNADPGDH I and BpNADPGDH II, are regulated by cAMP-dependent- and calmodulin (CaM) dependent protein kinases, respectively
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physiological function
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the rocG gene deletion mutant produces intracellular glutamic acid with a concentration of 90 ng/log (CFU), which is only 23.7% that of the wild-type. The poly-gamma.glutamic acid yield of the mutant is 5.37 g/l, a decrease of 45.3% compared to the wild type
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physiological function
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gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
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physiological function
-
glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
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physiological function
-
the gdh3/gdh3 mutant is able to grow on either arginine or proline as a sole carbon and nitrogen source, but the strain is locked in the yeast morphology in proline-containing medium. In proline medium, the gdh3/gdh3 mutant strain fails to form filaments, whilst the wild-type develops hyphae. Different concentrations of ATP, NAD+, NADH, NAPD+, NADPH, as well as 62 other metabolites, and 19 isotopically labelled are found metabolites between the mutant and the wild-type strains
-
physiological function
-
NADP-GDH isozyme Gdh3, but not Gdh1, mainly contributes to the oxidative stress resistance of stationary-phase cells. The insignificance of Gdh1 to stress resistance possibly results from conditional and reversible aggregation of Gdh1 into punctuate foci initiated in parallel with postdiauxic growth
-
physiological function
-
isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. Role of GDH1 and GDH2 (EC 1.4.1.2) in glutamate synthesis and its possible implication to oxidation stress defense through the glutathione system. GDH1 regulates chromatin through its catalytic activity. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The regulation of GDH1 under glucose conditions is performed by nitrogen catabolite repressor (NCR)-sensitive activators, Leu3p and activators exclusive for respiratory growth such as the HAP complex that coordinates nuclear and mitochondrial gene expression. Under ethanol conditions, GDH1 derepression is mediated by the Gcn4 and Hap4 transcriptional activators and is amplified by Gln3
-
physiological function
-
isozyme Gdh1 is the primary (hyperbolic) NADP-GDH enzyme and isozyme Gdh3 the cooperative NADP-GDH enzyme in the GDH pathway of Saccharomyces cerevisiae. The allosteric regulation of NADP-GDH activity is influenced by 2-oxoglutarate and NADP, and not by small molecules (e.g. GTP, AMP) or amino acids. Role of the GDH path in ROS-mediated apoptosis. GDH2 (EC 1.4.1.2) genetically interacts with GDH3 and controls stress-induced apoptosis. The transcription of GDH3 occurs extensively during the stationary phase. The activity of Gdh3p presents a 20 to 140fold increment when cells are grown under aerobic conditions. Under these conditions the majority of the total NADP-GDH activity is attributed to Gdh3p monomers that can contribute up to 70% to the pool, especially when cells enter or remain in aerobic metabolism for several days. Under acetate/raffinose conditions with ammonia as the only nitrogen source, yeast cells lacking GDH3 gene has a significant impairment in glutamate synthesis. The increase of the NADP-dependent GDH activity observed in gdh1DELTA mutants is presumably due to Gdh3p that seems to play a prominent role in glutamate metabolism under aerobic conditions. Glutamate synthesis under aerobic conditions is insufficient and requires additionally the activity of Gdh1p. The expression of both GDH3 and GDH1 is required to achieve wild-type growth in respiration. The transcriptional regulation of GDH3 is controlled by carbon sources and not by nitrogen catabolite repression as in the case of GDH1. The glucose-repressed expression of GDH3 is attributed to the condensed chromatin organization of its promoter
-
physiological function
-
gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable
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physiological function
-
glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica
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additional information
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview. A single sequence accommodates both coenzymes in the dual-specificity GDHs of animals
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
additional information
glucose starvation triggers the transition of the soluble form of Gdh1 into the insoluble aggregate form, which can be redissolved by replenishing glucose, without any requirement for protein synthesis
additional information
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glucose starvation triggers the transition of the soluble form of Gdh1 into the insoluble aggregate form, which can be redissolved by replenishing glucose, without any requirement for protein synthesis
additional information
P320 and C321 are both important for NADP+ binding
additional information
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glucose starvation triggers the transition of the soluble form of Gdh1 into the insoluble aggregate form, which can be redissolved by replenishing glucose, without any requirement for protein synthesis
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C141S
reductive amination activity of C141S alone is insensitive to treatment with 2-hydroxyethyl disulfide
C415S
mutant loses its reductive amination activity in a manner very similar to the native enzyme
K116A
almost complete loss of activity
K128A
almost complete loss of activity
K136A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
K92A
almost complete loss of activity
N347A
almost complete loss of activity
R208A
almost complete loss of activity
R290A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S265A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S379A
almost complete loss of activity
K116A
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almost complete loss of activity
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K128A
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almost complete loss of activity
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K92A
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almost complete loss of activity
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R208A
-
almost complete loss of activity
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S379A
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almost complete loss of activity
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K136A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
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R290A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
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S265A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
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C321A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+
K286Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L/S240A
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K341L
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity compared to wild-type
K92C
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 5.5fold increase in speific activity with homoserine
K92M
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 2.8fold increase in speific activity with homoserine
K92V
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 7.2fold increase in speific activity with homoserine
P320A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+. The mutant is not inhibited by propylselen
R289Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
R292Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K110L
a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
K419A
-
site-directed mutagenesis of GDH1
K420A
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site-directed mutagenesis of GDH1
K423A
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site-directed mutagenesis of GDH1
K426A
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site-directed mutagenesis of GDH1
K110L
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a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
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K419A
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site-directed mutagenesis of GDH1
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K420A
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site-directed mutagenesis of GDH1
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K423A
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site-directed mutagenesis of GDH1
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K426A
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site-directed mutagenesis of GDH1
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E158Q
-
3.3% as active as wild-type
T138E
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1.6% as active as wild-type
D167T
the mutant enzyme is slightly more thermostable than the wild-type enzyme
T138E
the mutant enzyme is much less thermostable than the wild-type enzyme
D167T
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the mutant enzyme is slightly more thermostable than the wild-type enzyme
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T138E
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the mutant enzyme is much less thermostable than the wild-type enzyme
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N117R
-
80% activity of wild-type at optimum temperature for catalysis
R190A/E231A/K193A
-
mutation has no effect on the overall conformation of the protein
S128R
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E
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120% activity of wild-type at optimum temperature for catalysis
S128R/T158E/N117R
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same activity as wild-type at optimum temperature for catalysis
S128R/T158E/N117R/S160E
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same activity as wild-type at optimum temperature for catalysis
S128R/T158E/S160E
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same activity as wild-type at optimum temperature for catalysis
T158E
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60% activity of wild-type at optimum temperature for catalysis
additional information
generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
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generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
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an active chimera (CEC) consisting of the substrate-binding domain (domain I) of CsGDH and the coenzyme-binding domain (domain II) of Escherichia coli GDH is generated. Kinetic constants of chimeric protein: Km values for substrates L-glutamate, 2-oxoglutarate, NH4Cl highly increased compared to wild-type, Vmax values also highly increased compared to wild-type. The CEC chimera, like Escherichia coli GDH, has a marked preference for NADP(H) as coenzyme. selectivity for the phosphorylated coenzyme does indeed reside solely in domain II. Positive cooperativity toward L-glutamate, characteristic of wild-type CsGDH, retains with domain I. Although glutamate cooperativity occurs only at higher pH values in the wild-tpye CsGDH, the chimeric protein shows it over the full pH range explored. The chimera is capable of catalyzing severalfold higher reaction rates (Vmax) in both directions than either of the parent enzymes from which it is constructed
additional information
chimeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
additional information
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gdh mutant TIL487, loss of ability to degrade amino acids
additional information
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gdh mutant TIL487, loss of ability to degrade amino acids
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additional information
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disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
additional information
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disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
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additional information
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deletion mutant lacking the first 19 amino acid residues, shows unchanged activity and forms hexamers, thus the unique extension does not appear to be essential for catalysis and subunit assembly, and presumably fulfils some other yet unknown function
additional information
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construction of enzyme deletion mutants DELTAgdh1 and DELTAgdh3, the mutants show less than 20% of wild-type activity, genotypes and phenotypes, overview
additional information
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promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
additional information
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
additional information
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mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
additional information
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mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
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additional information
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promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
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additional information
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overexpression of an NADP(H)-dependent glutamate dehydrogenase gene, TrGDH, from Trichurus sp. improves nitrogen assimilation, growth status, and grain weight per plant in rice, phenotype, overview. Compared with the rice GDH (OsGDH4), TrGDH exhibits higher affinity for NH4+
additional information
YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
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additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
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