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(2R,3R)-erythrofluoromalate + NAD+
?
-
-
-
-
?
(2S,3R)-tartrate + NAD+
?
-
-
-
-
?
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
(S)-malate + NAD+
pyruvate + CO2 + NADH
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
pyruvate + NADH + CO2
-
-
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
(S)-malate + NADP+
pyruvate + CO2 + NADPH
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
L-aspartate + NAD+
iminopyruvate + CO2 + NADH + H+
-
-
-
-
?
L-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
malate + NAD+
pyruvate + CO2 + NADH + H+
meso-tartrate + NAD+
?
-
-
-
-
?
pyruvate + CO2 + NADH
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
pyruvate + NAD+ + HCO3-
(S)-malate + NADH
additional information
?
-
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
-
-
-
-
?
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
-
-
-
-
r
(S)-malate + NAD+
?
-
-
-
-
?
(S)-malate + NAD+
?
-
the enzyme plays a special role in the decarboxylation of C4 acids to pyruvate and CO2, which are used in subsequent photosynthesis. pH, NAD+, and coenzyme A levels in the matrix act together to regulate (S)-malate oxidation
-
-
?
(S)-malate + NAD+
?
-
the enzyme plays a special role in the decarboxylation of C4 acids to pyruvate and CO2, which are used in subsequent photosynthesis. pH, NAD+, and coenzyme A levels in the matrix act together to regulate (S)-malate oxidation
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
the enzyme plays a central role in the metabolite flux through the tricarboxylic acid cycle, overview
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
the mitochondrial NAD-malic enzyme catalyzes the oxidative decarboxylation of malate to pyruvate and CO2
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
the NAD-malic enzyme catalyzes the oxidative decarboxylation of (S)-malate via oxaloacetate, Arg181 is within hydrogen bonding distance of the 1-carboxylate of malate in the active site of the enzyme and interacts with the carboxamide side chain of the nicotinamide ring of NADH, but not with NAD+
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
the decarboxylation reaction is preferred, overview
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
enzyme is involved in carbon fixation and metabolism, regulation of the pathways, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
mitochondrial isozyme ME2 responds to elevated amino acids and serves to supply sufficient pyruvate for increased Krebs cycle flux when glucose is limiting
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
the enzyme plays a role in symbiotic N2 fixation, overview
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
very low activity in the reverse reaction in vitro
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
Lacticaseibacillus casei BL23 and ATCC 334
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
Mnium undulatum
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
15% of the activity with NAD+
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
Crassula argentea
-
14% of the activity with NAD+
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
at 1.5% of the activity with NAD+
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
ir
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
-
r
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
NADP+ shows 22% of the activity with NAD+
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
NADP+ shows 22% of the activity with NAD+
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Amaranthus edulis
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
ionized malic acid is the true substrate
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
no decarboxylation of malate in absence of either Mg2+ or NAD+
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Crassula argentea
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Crassula argentea
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Crassula argentea
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Crassula argentea
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Crassula argentea
-
activity of the reverse reaction is 1.5% of that of the forward reaction
-
r
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
ir
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
Heliocarpus sp.
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
ir
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
r
malate + NAD+
pyruvate + CO2 + NADH + H+
salmon
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
ir
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
pyruvate + CO2 + NADH
(S)-malate + NAD+
-
the rate of carboxylation of pyruvate to malate is lower than for the decarboxylation reaction
-
-
r
pyruvate + CO2 + NADH
(S)-malate + NAD+
Crassula argentea
-
activity is 1.5% of the decarboxylation of (S)-malate
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate
-
-
r
pyruvate + NAD+ + HCO3-
(S)-malate + NADH
-
method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, from Leuconostoc mesenteroides
-
-
?
pyruvate + NAD+ + HCO3-
(S)-malate + NADH
-
method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, from Leuconostoc mesenteroides
-
-
?
additional information
?
-
-
NAD-ME1 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-ME1 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-ME1 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
-
NAD-ME2 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-ME2 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-ME2 does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
-
NAD-MEH does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-MEH does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-MEH does not perform decarboxylation of oxaloacetate
-
-
?
additional information
?
-
NAD-ME1 has a regulatory site for L-malate that can also bind fumarate
-
-
?
additional information
?
-
NAD-ME1 has a regulatory site for L-malate that can also bind fumarate
-
-
?
additional information
?
-
NAD-ME1 has a regulatory site for L-malate that can also bind fumarate. L-Malate binding to this site elicits a sigmoidal and low substrate-affinity response, whereas fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect is also observed when the allosteric site is either removed or altered. Fumarate is not really an activator, but suppresses the inhibitory effect of L-malate. Residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1
-
-
?
additional information
?
-
NAD-ME1 has a regulatory site for L-malate that can also bind fumarate. L-Malate binding to this site elicits a sigmoidal and low substrate-affinity response, whereas fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect is also observed when the allosteric site is either removed or altered. Fumarate is not really an activator, but suppresses the inhibitory effect of L-malate. Residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1
-
-
?
additional information
?
-
the enzyme is unable to decarboxylate oxaloacetate
-
-
-
additional information
?
-
the enzyme is unable to decarboxylate oxaloacetate
-
-
-
additional information
?
-
-
the Ascaris suum enzyme forms complexes with the structurally similar human enzyme
-
-
?
additional information
?
-
-
enzyme shows a strict requirement for 2S-stereochemistry
-
-
?
additional information
?
-
-
no decarboxylation of oxaloacetate
-
-
?
additional information
?
-
-
the enzyme is unable to decarboxylate oxaloacetate
-
-
-
additional information
?
-
Mnium undulatum
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
no decarboxylation of oxaloacetate
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
-
-
?
additional information
?
-
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
-
-
?
additional information
?
-
-
no decarboxylation of oxaloacetate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
(S)-malate + NAD+
pyruvate + CO2 + NADH
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
pyruvate + NADH + CO2
-
-
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
(S)-malate + NADP+
pyruvate + CO2 + NADPH
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
L-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
additional information
?
-
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
-
-
-
-
?
(S)-malate + NAD(P)+
pyruvate + CO2 + NAD(P)H
-
-
-
-
r
(S)-malate + NAD+
?
-
the enzyme plays a special role in the decarboxylation of C4 acids to pyruvate and CO2, which are used in subsequent photosynthesis. pH, NAD+, and coenzyme A levels in the matrix act together to regulate (S)-malate oxidation
-
-
?
(S)-malate + NAD+
?
-
the enzyme plays a special role in the decarboxylation of C4 acids to pyruvate and CO2, which are used in subsequent photosynthesis. pH, NAD+, and coenzyme A levels in the matrix act together to regulate (S)-malate oxidation
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
the enzyme plays a central role in the metabolite flux through the tricarboxylic acid cycle, overview
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
enzyme is involved in carbon fixation and metabolism, regulation of the pathways, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
mitochondrial isozyme ME2 responds to elevated amino acids and serves to supply sufficient pyruvate for increased Krebs cycle flux when glucose is limiting
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
the enzyme plays a role in symbiotic N2 fixation, overview
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
-
-
ir
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
Lacticaseibacillus casei BL23 and ATCC 334
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
Mnium undulatum
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
r
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + CO2 + NADPH
-
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
NADP+ shows 22% of the activity with NAD+
-
-
?
(S)-malate + NADP+
pyruvate + NADPH + H+ + CO2
NADP+ shows 22% of the activity with NAD+
-
-
?
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
-
-
-
r
pyruvate + CO2 + NADH + H+
(S)-malate + NAD+
-
the enzyme acts preferably in the direction of malate decarboxylation, the reverse reaction proceeds with much lower rate
-
-
r
additional information
?
-
-
the Ascaris suum enzyme forms complexes with the structurally similar human enzyme
-
-
?
additional information
?
-
Mnium undulatum
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
additional information
?
-
-
comparison of enzyme activity in different species under different conditions, significant differences in the accumulation of malate between day and night, overview
-
-
?
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Breast Neoplasms
Kinetic mechanism of the cytosolic malic enzyme from human breast cancer cell line.
Breast Neoplasms
Mitochondrial malic enzyme 2 promotes breast cancer metastasis via stabilizing HIF-1? under hypoxia.
Carcinoma
Expression of cytosolic malic enzyme (ME1) is associated with disease progression in human oral squamous cell carcinoma.
Carcinoma, Hepatocellular
Activities of enzymes of lipid metabolism in Morris hepatoma 7800 C1 cells.
Carcinoma, Hepatocellular
Purification, kinetic behavior, and regulation of NAD(P)+ malic enzyme of tumor mitochondria.
Corneal Dystrophies, Hereditary
Linkage analysis in granular corneal dystrophy (Groenouw I), Schnyder's crystalline corneal dystrophy, and Reis-Bücklers' corneal dystrophy.
Friedreich Ataxia
Cardiac malic enzyme in Friedreich's disease.
Friedreich Ataxia
Friedreich ataxia: III. Mitochondrial malic enzyme deficiency.
Friedreich Ataxia
Friedreich's ataxia: malic enzyme activity in cellular fractions of cultured skin fibroblasts.
Friedreich Ataxia
Friedreich's disease: IV. Reduced mitochondrial malic enzyme activity in heterozygotes.
Friedreich Ataxia
Mitochondrial malic enzyme in Friedreich's ataxia: failure to demonstrate reduced activity in cultured fibroblasts.
Friedreich Ataxia
Normal fibroblast mitochondrial malic enzyme activity in Friedreich's ataxia.
Friedreich Ataxia
Normal mitochondrial malic enzyme levels in Friedreich's ataxia fibroblasts.
glucose-6-phosphatase deficiency
Analysis of the albino-locus region of the mouse: IV. Characterization of 34 deficiencies.
Glycogen Storage Disease Type I
Analysis of the albino-locus region of the mouse: IV. Characterization of 34 deficiencies.
Insulinoma
Mitochondrial malic enzyme (ME2) in pancreatic islets of the human, rat and mouse and clonal insulinoma cells.
Leukemia
Enzyme activities of NADPH-forming metabolic pathways in normal and leukemic leukocytes.
Leukemia, Myeloid, Acute
Enzyme activities of NADPH-forming metabolic pathways in normal and leukemic leukocytes.
Malaria
Mitochondrial NAD+-dependent malic enzyme from Anopheles stephensi: a possible novel target for malaria mosquito control.
malate dehydrogenase (decarboxylating) deficiency
Friedreich ataxia: III. Mitochondrial malic enzyme deficiency.
malate dehydrogenase (decarboxylating) deficiency
Friedreich's ataxia: malic enzyme activity in cellular fractions of cultured skin fibroblasts.
malate dehydrogenase (decarboxylating) deficiency
Genomic deletion of malic enzyme 2 confers collateral lethality in pancreatic cancer.
malate dehydrogenase (oxaloacetate-decarboxylating) deficiency
Friedreich ataxia: III. Mitochondrial malic enzyme deficiency.
Melanoma
Metabolic Vulnerability in Melanoma: A ME2 (Me Too) Story.
Neoplasm Metastasis
Mitochondrial malic enzyme 2 promotes breast cancer metastasis via stabilizing HIF-1? under hypoxia.
Neoplasms
Characterization of cytosolic malic enzyme in human tumor cells.
Neoplasms
Kinetic mechanism of the cytosolic malic enzyme from human breast cancer cell line.
Neoplasms
Malic enzyme and malate dehydrogenase activities in rat tracheal epithelial cells during the progression of neoplasia.
Neoplasms
Nuclear thyroid hormone receptors, alpha-glycerophosphate dehydrogenases, and malic enzyme in N-nitrosomethylurea-induced rat mammary tumors.
Neoplasms
Purification and characterization of the cytosolic NADP(+)-dependent malic enzyme from human breast cancer cell line.
Neoplasms
Purification of tumor mitochondrial malic enzyme by specific ligand affinity chromatography.
Neoplasms
The pathways of glutamate and glutamine oxidation by tumor cell mitochondria. Role of mitochondrial NAD(P)+-dependent malic enzyme.
Squamous Cell Carcinoma of Head and Neck
Expression of cytosolic malic enzyme (ME1) is associated with disease progression in human oral squamous cell carcinoma.
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2
(2R,3R)-erythrofluoromalate
-
25°C
20
(2S,3R)-tartrate
-
25°C, pH 7.8
40
meso-tartrate
-
25°C, pH 7.8
additional information
additional information
-
0.003
(S)-malate
-
isoform ME2, at pH 6.5 and 37°C
0.0035
(S)-malate
-
isoform ME1, at pH 6.5 and 37°C
0.1
(S)-malate
-
with NAD+ as cofactor
0.16
(S)-malate
-
pH 7.5, 25°C
0.458
(S)-malate
-
with NADP+ as cofactor
0.5
(S)-malate
-
pH 7.0, 25°C, mutant N434A, in presence of Mn2+
0.53
(S)-malate
-
pH 8.5, 25°C, recombinant wild-type enzyme
0.59
(S)-malate
Crassula argentea
-
activation by Mn2+
0.59
(S)-malate
pH 7.8, 30°C, AZC3656, in presence of 1 mM fumarate
0.64
(S)-malate
pH 7.8, 30°C, AZC3656, in presence of 10 mM succinate
0.76
(S)-malate
-
with NAD+ and Mn2+
0.8
(S)-malate
Crassula argentea
-
activation by Mn2+
0.8
(S)-malate
-
pH 7.0, 25°C, wild-type enzyme
1.3
(S)-malate
-
pH 7.0, 25°C, mutant S433A
1.7
(S)-malate
-
pH 7.0, 25°C, mutant N479S
1.7
(S)-malate
pH 7.2, 30°C, with NAD+
1.8
(S)-malate
-
pH 7.0, 25°C, mutant N479Q
2 - 3
(S)-malate
-
pH 8.5, 25°C, recombinant mutant R181Q in presence of 60 mM guanidinium
2.2
(S)-malate
-
pH 7.0, 25°C, mutant N434M
2.6
(S)-malate
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
2.7
(S)-malate
pH 6.5, temperature not specified in the publication, NAD-MEH
2.7
(S)-malate
pH 7.8, 30°C, AZC3656
3
(S)-malate
pH 7.4, 30°C, isozyme NAD-ME1
3
(S)-malate
pH 7.4, 30°C, isozyme NAD-ME2
3
(S)-malate
pH 6.4, temperature not specified in the publication, NAD-ME1
3
(S)-malate
pH 6.6, temperature not specified in the publication, NAD-ME2
3.2
(S)-malate
-
with NAD+ as coenzyme, activation by Mn2+
4.2
(S)-malate
-
with NADP+ and Mn2+
4.3
(S)-malate
-
pH 7.0, 25°C, mutant N434Q
5.97
(S)-malate
-
with NAD+ as coenzyme
6.03
(S)-malate
Crassula argentea
-
activation by Mg2+
8
(S)-malate
-
pH 8.5, 25°C, recombinant mutant R181Q, in presence of 60 mM NH4+
8.1
(S)-malate
-
pH 8.0, 30°C, recombinant enzyme
8.34
(S)-malate
-
with NADP+ as coenzyme
9.8
(S)-malate
-
with NADP+ as coenzyme, activation by Mn2+
12.3
(S)-malate
-
with NADP+ and Mg2+
13
(S)-malate
-
with NAD+ as coenzyme, activation by Mg2+
14
(S)-malate
-
with NAD+ and Mg2+
15
(S)-malate
pH 7.2, 30°C, with NADP+
22.5
(S)-malate
-
with NADP+ as coenzyme, activation by Mg2+
27.6
(S)-malate
pH 7.8, 30°C, AZC3656, in presence of 0.05 mM acetyl-CoA
50
(S)-malate
-
pH 8.5, 25°C, recombinant mutant R181Q
57
(S)-malate
-
pH 8.5, 25°C, recombinant mutant R181K
13.48
CO2
Crassula argentea
-
activation by Mg2+
0.00035
NAD+
-
isoform ME1, at pH 6.5 and 37°C
0.00037
NAD+
-
isoform ME2, at pH 6.5 and 37°C
0.035
NAD+
-
pH 8.5, 25°C, recombinant wild-type enzyme
0.07
NAD+
-
pH 8.5, 25°C, recombinant mutant R181Q
0.1
NAD+
-
activation by Mn2+
0.101
NAD+
pH 7.8, 30°C, AZC3656
0.11
NAD+
pH 7.2, 30°C, with (S)-malate
0.47
NAD+
-
with 30 mM Mg2+
0.48
NAD+
-
with 8 mM Mg2+
0.5
NAD+
-
activation by Mn2+
0.5
NAD+
-
with 80 mM Mg2+
0.5
NAD+
pH 7.4, 30°C, isozyme NAD-ME1
0.5
NAD+
pH 7.4, 30°C, isozyme NAD-ME2
0.5
NAD+
pH 6.4, temperature not specified in the publication, NAD-ME1
0.5
NAD+
pH 6.6, temperature not specified in the publication, NAD-ME2
0.55
NAD+
pH 6.5, temperature not specified in the publication, NAD-MEH
0.77
NAD+
Crassula argentea
-
activation by Mg2+
0.8
NAD+
-
pH 7.0, 25°C, wild-type enzyme
0.82
NAD+
-
activation by Mg2+
0.9
NAD+
-
activation by Mg2+
1.1
NAD+
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
1.6
NAD+
-
pH 7.0, 25°C, mutant S433A
1.7
NAD+
-
pH 7.0, 25°C, mutant N479S
1.8
NAD+
-
pH 7.0, 25°C, mutant N479Q
2
NAD+
-
pH 7.0, 25°C, mutant N434A, in presence of Mn2+
3
NAD+
-
pH 7.0, 25°C, mutant N434M
4.3
NAD+
-
pH 8.0, 30°C, recombinant enzyme
5
NAD+
-
pH 7.0, 25°C, mutant N434Q
0.00015
NADH
-
isoform ME1, at pH 6.5 and 37°C
0.00018
NADH
-
isoform ME2, at pH 6.5 and 37°C
0.12
NADH
Crassula argentea
-
activation by Mn2+
0.207
NADP+
-
-
0.3
NADP+
-
activation by Mn2+
1.32
NADP+
-
activation by Mn2+
1.7
NADP+
-
with NADP+ as coenzyme
1.8
NADP+
pH 7.2, 30°C, with (S)-malate
2.1
NADP+
pH 7.8, 30°C, AZC3656
6.12
NADP+
-
activation by Mg2+
0.00125
pyruvate
-
isoform ME2, at pH 6.5 and 37°C
0.00158
pyruvate
-
isoform ME1, at pH 6.5 and 37°C
4.1
pyruvate
-
pH 7.0, 25°C
15.03
pyruvate
Crassula argentea
-
activation by Mn2+
additional information
additional information
-
-
-
additional information
additional information
Crassula argentea
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
detailed kinetic mechanism study, steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, primary deuterium and 13C isotope effects of mutant R181Q in the absence and presence of ammonium ions, overview
-
additional information
additional information
-
primary deuterium and 13C kinetic isotope effects, kinetics, and kinetic mechanism of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic analysis and comparison of the different isozymes MAD-ME1, NAD-ME2, and NAD-MEH, and of mutants NADME1q and NAD-ME2q, overview
-
additional information
additional information
kinetic analysis and comparison of the different isozymes MAD-ME1, NAD-ME2, and NAD-MEH, and of mutants NADME1q and NAD-ME2q, overview
-
additional information
additional information
kinetic analysis and comparison of the different isozymes MAD-ME1, NAD-ME2, and NAD-MEH, and of mutants NADME1q and NAD-ME2q, overview
-
additional information
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
-
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
-
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
-
additional information
additional information
-
kinetics analysis of isozymes ME2 and ME3
-
additional information
additional information
Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and presents a sigmoidal kinetic response for L-malate. Fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme, overview
-
additional information
additional information
Arabidopsis NAD-ME1 exhibits a non-hyperbolic behavior for the substrate L-malate and presents a sigmoidal kinetic response for L-malate. Fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme, overview
-
additional information
additional information
NAD-ME2 shows a typical hyperbolic behavior
-
additional information
additional information
NAD-ME2 shows a typical hyperbolic behavior
-
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malfunction
dme mutants of the broad-host-range Sinorhizobium sp. strain NGR234 form nodules whose level of N2 fixation vary from 27 to 83% (plant dry weight) of the wild-type level, depending on the host plant inoculated. The single dme mutant fixes N2 at reduced rate. A pckA dme double mutant has no N2-fixing activity, PCK is phosphoenolpyruvate carboxykinase. Symbiotic phenotypes of NGR234 and NGR234 dme mutants on different host plants, overview
malfunction
-
the single Sco2951 and the double Sco2951 Sco5261 mutants, deficient in ME-NAD and ME-NADP, EC 1.1.1.40, activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglycerides during exponential growth
malfunction
-
knockdown of ME1 does not inhibit insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine
malfunction
-
the single Sco2951 and the double Sco2951 Sco5261 mutants, deficient in ME-NAD and ME-NADP, EC 1.1.1.40, activity, display a strong reduction in the production of the polyketide antibiotic actinorhodin. Additionally, the Sco2951/Sco5261 mutant shows a decrease in stored triacylglycerides during exponential growth
-
malfunction
-
dme mutants of the broad-host-range Sinorhizobium sp. strain NGR234 form nodules whose level of N2 fixation vary from 27 to 83% (plant dry weight) of the wild-type level, depending on the host plant inoculated. The single dme mutant fixes N2 at reduced rate. A pckA dme double mutant has no N2-fixing activity, PCK is phosphoenolpyruvate carboxykinase. Symbiotic phenotypes of NGR234 and NGR234 dme mutants on different host plants, overview
-
metabolism
-
the citrate-malate-pyruvate cycle serves to regenerate NAD+ and maintain glycolytic flux. Pyruvate cycles all lead to the exchange of reducing equivalents from mitochondrial NADH to cytosolic NADPH. Malic enzyme is integral to the coupling of metabolism with insulin secretion
metabolism
-
the malic enzyme is involved in the (S)-malate catabolic pathways and the putative gluconeogenic pathways, overview
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
-
fish spermatozoa contain a glycolytic pathway, tricarboxylic acid cycle and oxidative phosphorylation system, all of which are key pathways contributing to ATP synthesis, involving the enzyme
metabolism
Lacticaseibacillus casei BL23 and ATCC 334
-
the malic enzyme is involved in the (S)-malate catabolic pathways and the putative gluconeogenic pathways, overview
-
physiological function
for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1
physiological function
malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
physiological function
-
siRNA knockdown and isotopic labeling strategies to evaluate the role of cytosolic and mitochondrial isozymes of malic enzyme in facilitating malate-pyruvate cycling in the context of fuel-stimulated insulin secretion, overview
physiological function
-
the malic enzyme pathway enables Lactobacillus casei to grow on L-malic acid., requirement of the MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway, overview
physiological function
AZC3656 protein is a NAD+-malic enzyme, i.e. DME, while AZC0119 protein is not a malic enzyme. DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate. But NGR234 bacteroids appear to synthesize pyruvate from TCA cycle intermediates via DME or PCK, phosphoenolpyruvate carboxykinase, pathways, overview
physiological function
-
DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate
physiological function
-
the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
physiological function
plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME). Malic enzyme tracers reveal hypoxia-induced switch in adipocyte NADPH pathway usage
physiological function
Plant mitochondria can use L-malate and fumarate, which accumulate in large levels, as respiratory substrates. In part, this property is due to the presence of NAD-dependent malic enzymes (NAD-ME). Malic enzyme tracers reveal hypoxia-induced switch in adipocyte NADPH pathway usage. Important role of NAD-ME1 in processes that control flow of C4 organic acids in Arabidopsis mitochondrial metabolism.. NAD-ME1 exhibits a complex homo and heterotrophic allosteric regulation with L-malate wielding an inhibitory effect that is cancelled by competitive fumarate binding
physiological function
Lacticaseibacillus casei BL23 and ATCC 334
-
the malic enzyme pathway enables Lactobacillus casei to grow on L-malic acid., requirement of the MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway, overview
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physiological function
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malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
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physiological function
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the enzyme plays a role in antibiotic and triacylglycerol production, e.g. production of the polyketide antibiotic actinorhodin, overview
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physiological function
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AZC3656 protein is a NAD+-malic enzyme, i.e. DME, while AZC0119 protein is not a malic enzyme. DME is considered an important enzyme for regulating C4-dicarboxylic acid metabolism in N2-fixing bacteroids because its activity is strongly inhibited by acetyl-CoA and stimulated by fumarate and succinate. The NAD+-malic enzyme is required for N2 fixation, and this activity is thought to be required for the anaplerotic synthesis of pyruvate. But NGR234 bacteroids appear to synthesize pyruvate from TCA cycle intermediates via DME or PCK, phosphoenolpyruvate carboxykinase, pathways, overview
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additional information
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deletion of either the gene encoding the histidine kinase or the response regulator of the TC system results in the loss of the ability to grow on L-malic acid, thus indicating that the cognate TC system regulates and is essential for the expression of malic enzyme. Expression of maeE is induced in the presence of L-malic acid and repressed by glucose, whereas TC system expression is induced by L-malic acid and is not repressed by glucose
additional information
enzyme activity is allosterically regulated by acetyl-CoA
additional information
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higher expression of ME2 correlates with the degree of cell de-differentiation. Knockdown of ME2 leads to induction of erythroid differentiation, and diminished proliferation of tumor cells and increased apoptosis in vitro. ME2 knockdown also totally abolishes growth of K562 cells in nude mice. Depletion of endogenous ME2 levels enhances reactive oxygen species, increases NAD+/NADH and NADP+/NADPH ratio and inhibits ATP production in K562 cells. ME2 depletion resulted in high orotate levels, suggesting potential impairment of pyrimidine metabolism
additional information
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identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
identification of specific domains of the primary structure, which are involved in the differential allosteric regulation. Different properties of NAD-ME1, -2, and -H, mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles, overview
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. Mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
residues Arg50, Arg80 and Arg84 show different roles in organic acid binding. These residues form a triad, which is the basis of the homo and heterotrophic effects that characterize NAD-ME1. Mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview
additional information
Lacticaseibacillus casei BL23 and ATCC 334
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deletion of either the gene encoding the histidine kinase or the response regulator of the TC system results in the loss of the ability to grow on L-malic acid, thus indicating that the cognate TC system regulates and is essential for the expression of malic enzyme. Expression of maeE is induced in the presence of L-malic acid and repressed by glucose, whereas TC system expression is induced by L-malic acid and is not repressed by glucose
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additional information
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enzyme activity is allosterically regulated by acetyl-CoA
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R50A
site-directed mutagenesis, the mutant does not show altered kinetics after addition of fumarate
R80A
site-directed mutagenesis, the mutant shows altered kinetics after addition of fumarate
R84A
site-directed mutagenesis, the mutant does not show altered kinetics after addition of fumarate
K143A
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site-directed mutagenesis, malate binding residue, mutant shows highly increased kcat for malate and fumarate compared to the wild-type enzyme
K362H
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the mutant enzyme displays a considerable elevation in Km for NADP+, and the kcat for NAD+ value is elevated compared to the wild-type enzyme
N434A
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site-directed mutagenesis, the interaction of the 434 position residue with malate is lost in the mutant, causing malate to reorient itself, leading to a slower decarboxylation
N434E
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site-directed mutagenesis, the longer glutamine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
N434M
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site-directed mutagenesis, the longer methionine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
N479Q
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site-directed mutagenesis, the stepwise oxidative decarboxylation mechanism observed for the wild-type enzyme changed to a concerted one, which is totally rate limiting, for the N479Q mutant enzyme
N479S
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site-directed mutagenesis, the mutant with the shorter serine side chain shows very similar values of KNAD+, Kmalate, and isotope effects relative to the wild-type enzyme, but V/Et is decreased 2000fold due to an increased freedom of rotation, resulting in nonproductively bound cofactor
R105A
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site-directed mutagenesis, fumarate binding residue, mutant shows 7-8fold reduced initial velocity with malate and Mg2+ compared to the wild-type enzyme, and is no longer activated by fumarate and malate
R181K
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site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme
R181Q
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site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme. The activity of the R181Q mutant can be partially rescued by ammonium ion likely by binding in the pocket vacated by the guanidinium group of R181
S433A
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site-directed mutagenesis, KNAD+ for the S433A mutant enzyme is increased by 80fold compared to the wild-type enzyme
S433C
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site-directed mutagenesis, the mutant enzyme exhibits 9fold and 500fold increases in Kmalate and KNAD, respectively, compared to the wild-type enzyme
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
additional information
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construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
construction of two chimeras NADME1q and NAD-ME2q by interchanging the first 176 amino residues between NAD-ME1 and -2, altered regulation in comparison to the wild-type enzymes, overview
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of chimeric protein NAD-ME1q, which is composed of the first 176 amino acid residues of isozyme NAD-ME2 and the central and C-terminal sequence of isozyme NAD-ME1, exhibits a significantly lower Km L-malate value than the parental isoforms and a hyperbolic behavior that is not modified by fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of chimeric protein NAD-ME1q, which is composed of the first 176 amino acid residues of isozyme NAD-ME2 and the central and C-terminal sequence of isozyme NAD-ME1, exhibits a significantly lower Km L-malate value than the parental isoforms and a hyperbolic behavior that is not modified by fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of the chimeric protein NAD-ME2q, that possesses the first 176 amino acid residues of NAD-ME1 and the central and C-terminal sequence of NAD-ME2, presents a sigmoidal L-malate response similar to the one for NAD-ME1, but also a higher Km L-malate value and a lower kcat value. NAD-ME2q is activated by fumarate and an increase in its concentration produces a decrease in Km and nH values. At 4 mM fumarate, the Lmalate saturation curve is hyperbolic (nH = 1.1) with an 8fold decrease in Km value. There are no significant changes in kcat value by addition of fumarate, which implies a 9fold increase in NAD-ME2q catalytic efficiency when compared to the enzyme in the absence of fumarate
additional information
mutants and chimeric proteins of NAD-ME1 and -2 indicated that the amino-terminal region of NAD-ME1 is implicated in fumarate activation and sigmoidal L-malate responses, structure-function analysis, overview. Generation of the chimeric protein NAD-ME2q, that possesses the first 176 amino acid residues of NAD-ME1 and the central and C-terminal sequence of NAD-ME2, presents a sigmoidal L-malate response similar to the one for NAD-ME1, but also a higher Km L-malate value and a lower kcat value. NAD-ME2q is activated by fumarate and an increase in its concentration produces a decrease in Km and nH values. At 4 mM fumarate, the Lmalate saturation curve is hyperbolic (nH = 1.1) with an 8fold decrease in Km value. There are no significant changes in kcat value by addition of fumarate, which implies a 9fold increase in NAD-ME2q catalytic efficiency when compared to the enzyme in the absence of fumarate
additional information
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method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides
additional information
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method optimization of the reverse reaction of the malic enzyme for HCO3- fixation into pyruvic acid to produce L-malic acid with NADH generation including the activity of glucose-6-phosphate dehydrogenase, EC1.1.1.49, from Leuconostoc mesenteroides
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additional information
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stable knockdown of ME2 in K-562 tumor cells using three independent shRNA hairpins targeting ME2, effects on K562 cell proliferation, knockout of ME2 induces erythroid differentiation, phenotype, detailed overview
additional information
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siRNA knockdown of malic enzyme isozyme by 50% affects pyruvate carboxylase flux of the pyruvate derived from glutamate metabolism, insulin secretion in response to membrane depolarization using potassium chloride is unaffected by siRNA knockdown of malic enzyme, overview
additional information
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siRNA knockout of ME2 in INS-1 832/13 beta-cells, siRNA knockdown and isotopic labeling strategies, method optimization, overview
additional information
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generation of Me1 single and double knockdown cell lines, thereby generating cell line 753(H)/Me1-753(P), overview. The level of Me1 mRNA in the double-knockdown cell line Me1-753(H)/Me1-753(P) is decreased to 2% as compared with 14% in the single knockdown Me1-753(H) cell line. The level of Me2mRNAis lowered by only 10% in the Me1-753(H) cell line and Me3 mRNA is lowered by only 27% in the Me1-753(H) cell line and lowered by only 35% in the Me1-753(H)/Me1-753(P) cell line. Resident siRNA might interfere with the expression of the siRNA expressed from the second vector. Knockdown of isozyme ME3, EC 1.1.1.40, but not ME1 or ME2 (both EC 1.1.1.39) alone or together, inhibits insulin release stimulated by glucose, pyruvate or 2-aminobicyclo [2,2,1]heptane-2-carboxylic acid-plus-glutamine. In the Me3 double-knockdown cells, the level of Me1 mRNA is not significantly decreased in the Me3-628(P)/Me2-725(H) and Me3-1672(P)/Me2-725(H) cell lines. However, a 32%, 49%, and 47% decrease in ME1 activity is observed in the cell lines Me3-628(P), Me3-628(P)/Me2-725(H), and Me3-628(P)/Me2-2124(H), respectively
additional information
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expression of the tme gene, EC 1.1.1.40, under the control of the dme promoter, cannot restore the N2 fixation activity which is lost in dme mutant cells in alfalfa root nodules, despite elevated levels of TME within bacteroids, no symbiotic nitrogen fixation occurs in dme mutant strains, overview
additional information
azc3656 mutants show about 4fold reduced NAD+-malic enzyme activity
additional information
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azc3656 mutants show about 4fold reduced NAD+-malic enzyme activity
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Atriplex spongiosa, Brassica oleracea, Crassula argentea, Solanum tuberosum
-
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Evidence for a multiple subunit composition of plant NAD malic enzyme
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Crassula argentea, Solanum tuberosum
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Brassica oleracea, Solanum tuberosum
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Brassica oleracea
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Characterization of two members of a novel malic enzyme class
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Sinorhizobium meliloti
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Wedding, R.T.; Black, M.K.
Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea
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Crassula argentea
brenda
Hatch, M.D.; Tsuzuki, M.; Edwards, G.E.
Determination of NAD malic enzyme in leaves of C4 plants
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Amaranthus retroflexus
brenda
Wedding, R.T.; Canellas, P.F.; Black, M.K.
Slow transients in the activity of the NAD malic enzyme from Crassula
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Crassula argentea
brenda
Grover, S.D.; Canellas, P.F.; Wedding, R.T.
Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties
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209
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Solanum tuberosum
brenda
Canellas, P.F.; Wedding, R.T.
Substrate and metal ion interactions in the NAD+ malic enzyme from cauliflower
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199
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Brassica oleracea
brenda
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Nicotinamide-adenine dinucleotide-linked malic enzyme in flight muscle of the tse-tse fly (Glossina) and other insects
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Apis mellifera, Schistocerca gregaria, Glossina austeni, Glossina longipennis, Glossina morsitans, Glossina pallidipes, Heliocarpus sp., Odontotermes sp., Periplaneta americana, Sarcophaga sp., Spodoptera exempta
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Hatch, M.D.; Mau, S.L.; Kagawa, T.
Properties of leaf NAD malic enzyme from plants with C4 pathway photosynthesis
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Amaranthus edulis, Atriplex spongiosa, Panicum miliaceum
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Bos taurus, Gadidae, Homo sapiens, salmon
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Oryctolagus cuniculus
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Two malic enzymes in Pseudomonas aeruginosa
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Pseudomonas aeruginosa
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Purification and partial characterization of malate dehydrogenase (decarboxylating) from Tritrichomonas foetus hydrogenosomes
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1993
Tritrichomonas suis
brenda
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Purification and properties of malic enzyme from Pseudomonas diminuta IFO-13182
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Brevundimonas diminuta
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brenda
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Purification and partial characterization of NAD-dependent malic enzyme isolated from Vigna unguiculata hypocotyls
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1996
Vigna unguiculata
-
brenda
Chen, F.; Okabe, Y.; Osano, K.; Tajima, S.
Purification and characterization of an NAD-malic enzyme from Bradyrhizobium japonicum A1017
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Bradyrhizobium japonicum
brenda
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Alternative substrates for malic enzyme: oxidative decarboxylation of L-aspartate
Biochemistry
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2002
Ascaris suum
brenda
Coleman, D.E.; Rao, G.S.; Goldsmith, E.J.; Cook, P.F.; Harris, B.G.
Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution
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Ascaris suum
brenda
Karsten, W.E.; Pais, J.E.; Rao, G.S.; Harris, B.G.; Cook, P.F.
Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites
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Ascaris suum
brenda
Rao, G.S.J.; Coleman, D.E.; Karsten, W.E.; Cook, P.F.; Harris, B.G.
Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site
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Ascaris suum
brenda
Lara, M.V.; Drincovich, M.F.; Andreo, C.S.
Induction of a crassulacean acid-like metabolism in the C(4) succulent plant, Portulaca oleracea L: study of enzymes involved in carbon fixation and carbohydrate metabolism
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Portulaca oleracea
brenda
Kuo, C.W.; Hung, H.C.; Tong, L.; Chang, G.G.
Metal-induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzyme
Proteins
54
404-411
2004
Homo sapiens
brenda
Tao, X.; Yang, Z.; Tong, L.
Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism
Structure
11
1141-1150
2003
Homo sapiens
brenda
Mitsch, M.J.; Cowie, A.; Finan, T.M.
Malic Enzyme Cofactor and Domain Requirements for Symbiotic N2-fixation by Sinorhizobium meliloti
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Sinorhizobium meliloti
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Karsten, W.E.; Cook, P.F.
Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum
Biochemistry
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Ascaris suum
brenda
Aktas, D.F.; Cook, P.F.
Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction
Biochemistry
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2008
Ascaris suum
brenda
Chang, H.C.; Chen, L.Y.; Lu, Y.H.; Li, M.Y.; Chen, Y.H.; Lin, C.H.; Chang, G.G.
Metal ions stabilize a dimeric molten globule state between the open and closed forms of malic enzyme
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Homo sapiens
brenda
Ohno, Y.; Nakamori, T.; Zheng, H.; Suye, S.
Reverse reaction of malic enzyme for HCO3- fixation into pyruvic acid to synthesize L-malic acid with enzymatic coenzyme regeneration
Biosci. Biotechnol. Biochem.
72
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2008
Brevundimonas diminuta, Brevundimonas diminuta IFO 13182
brenda
Pongratz, R.L.; Kibbey, R.G.; Shulman, G.I.; Cline, G.W.
Cytosolic and mitochondrial malic enzyme isoforms differentially control insulin secretion
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282
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2007
Rattus norvegicus
brenda
Tronconi, M.A.; Fahnenstich, H.; Gerrard Weehler, M.C.; Andreo, C.S.; Fluegge, U.I.; Drincovich, M.F.; Maurino, V.G.
Arabidopsis NAD-malic enzyme functions as a homodimer and heterodimer and has a major impact on nocturnal metabolism
Plant Physiol.
146
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2008
Arabidopsis thaliana (Q8L7K9), Arabidopsis thaliana (Q9SIU0)
brenda
Landete, J.M.; Garcia-Haro, L.; Blasco, A.; Manzanares, P.; Berbegal, C.; Monedero, V.; Zuniga, M.
Requirement of the Lactobacillus casei MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway
Appl. Environ. Microbiol.
76
84-95
2010
Lacticaseibacillus casei, Lacticaseibacillus casei BL23 and ATCC 334
brenda
Tronconi, M.A.; Gerrard Wheeler, M.C.; Maurino, V.G.; Drincovich, M.F.; Andreo, C.S.
NAD-malic enzymes of Arabidopsis thaliana display distinct kinetic mechanisms that support differences in physiological control
Biochem. J.
430
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2010
Arabidopsis thaliana (Q8L7K9), Arabidopsis thaliana (Q9SIU0), Arabidopsis thaliana
brenda
Sato, I.; Yoshikawa, J.; Furusawa, A.; Chiku, K.; Amachi, S.; Fujii, T.
Isolation and properties of malic enzyme and its gene in Rhodopseudomonas palustris No. 7
Biosci. Biotechnol. Biochem.
74
75-81
2010
Rhodopseudomonas palustris (A4F2S6), Rhodopseudomonas palustris No. 7 (A4F2S6)
brenda
Tronconi, M.A.; Maurino, V.G.; Andreo, C.S.; Drincovich, M.F.
Three different and tissue-specific NAD-malic enzymes generated by alternative subunit association in Arabidopsis thaliana
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285
11870-11879
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Arabidopsis thaliana, Arabidopsis thaliana (Q8L7K9), Arabidopsis thaliana (Q9SIU0)
brenda
Pongratz, R.L.; Kibbey, R.G.; Cline, G.W.
Investigating the roles of mitochondrial and cytosolic malic enzyme in insulin secretion
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457
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Rattus norvegicus
brenda
Rzepka, A.; Rut, G.; Krupa, J.
Effect of abiotic stress factors on fluctuations in contents of malate and citrate and on malic enzyme activity in moss gametophores
Photosynthetica
47
141-145
2009
Pilosella officinarum, Polytrichum commune, Polytrichum piliferum, Mnium undulatum
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brenda
Ren, J.G.; Seth, P.; Everett, P.; Clish, C.B.; Sukhatme, V.P.
Induction of erythroid differentiation in human erythroleukemia cells by depletion of malic enzyme 2
PLoS ONE
5
e12520
2010
Homo sapiens
brenda
Zhang, Y.; Aono, T.; Poole, P.; Finan, T.M.
NAD(P)+-malic enzyme mutants of Sinorhizobium sp. strain NGR234, but not Azorhizobium caulinodans ORS571, maintain symbiotic N2 fixation capabilities
Appl. Environ. Microbiol.
78
2803-2812
2012
Azorhizobium caulinodans, Sinorhizobium sp. (B6E9W4), Sinorhizobium sp. NGR234 (B6E9W4)
brenda
Rodriguez, E.; Navone, L.; Casati, P.; Gramajo, H.
Impact of malic enzymes on antibiotic and triacylglycerol production in Streptomyces coelicolor
Appl. Environ. Microbiol.
78
4571-4579
2012
Streptomyces coelicolor, Streptomyces coelicolor M145
brenda
Fu, Z.; Zhang, Z.; Liu, Z.; Hu, X.; Xu, P.
The effects of abiotic stresses on the NADP-dependent malic enzyme in the leaves of the hexaploid wheat
Biol. Plant.
55
196-200
2011
Triticum aestivum (A9LIN4), Triticum aestivum Jinmai 47 (A9LIN4)
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brenda
Niedzwiecka, N.; Skorkowski, E.F.
Purification and properties of malic enzyme from herring Clupea harengus spermatozoa
Comp. Biochem. Physiol. B
164
216-220
2013
Cyprinus carpio, Clarias gariepinus, Clupea harengus, Salmo salar, Salmo trutta
brenda
Hsieh, J.Y.; Chen, M.C.; Hung, H.C.
Determinants of nucleotide-binding selectivity of malic enzyme
PLoS ONE
6
e25312
2011
Ascaris suum
brenda
Niedzwiecka, N.; Gronczewska, J.; Skorkowski, E.F.
NAD-preferring malic enzyme: localization, regulation and its potential role in herring (Clupea harengus) sperm cells
Fish Physiol. Biochem.
43
351-360
2017
Clupea harengus
brenda
Hasan, N.M.; Longacre, M.J.; Stoker, S.W.; Kendrick, M.A.; MacDonald, M.J.
Mitochondrial malic enzyme 3 is important for insulin secretion in pancreatic beta-cells
Mol. Endocrinol.
29
396-410
2015
Rattus norvegicus
brenda
Tronconi, M.A.; Wheeler, M.C.; Martinatto, A.; Zubimendi, J.P.; Andreo, C.S.; Drincovich, M.F.
Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate
Phytochemistry
111
37-47
2015
Arabidopsis thaliana (Q8L7K9), Arabidopsis thaliana (Q9SIU0)
brenda
Babayev, H.; Mehvaliyeva, U.; Aliyeva, M.; Feyziyev, Y.; Guliyev, N.
The study of NAD-malic enzyme in Amaranthus cruentus L. under drought
Plant Physiol. Biochem.
81
84-89
2014
Amaranthus cruentus
brenda
Tronconi, M.A.; Andreo, C.S.; Drincovich, M.F.
Chimeric structure of plant malic enzyme family Different evolutionary scenarios for NAD- and NADP-dependent isoforms
Front. Plant Sci.
9
565
2018
Arabidopsis thaliana (Q8L7K9), Arabidopsis thaliana (Q9SIU0)
brenda
Wen, Z.; Zhang, M.
Possible involvement of phosphoenolpyruvate carboxylase and NAD-malic enzyme in response to drought stress. A case study a succulent nature of the C4-NAD-ME type desert plant, Salsola lanata (Chenopodiaceae)
Funct. Plant Biol.
44
1219-1228
2017
Climacoptera lanata
brenda
Eprintsev, A.T.; Fedorin, D.N.; Gataullina, M.O.; Igamberdiev, A.U.
Two forms of NAD-malic enzyme in maize leaves are regulated by light in opposite ways via promoter methylation
J. Plant Physiol.
251
153193
2020
Zea mays
brenda
Watson-Lazowski, A.; Papanicolaou, A.; Sharwood, R.; Ghannoum, O.
Investigating the NAD-ME biochemical pathway within C4 grasses using transcript and amino acid variation in C4 photosynthetic genes
Photosynth. Res.
138
233-248
2018
Panicum virgatum, Panicum coloratum, Disakisperma dubium, Diplachne fusca, Astrebla pectinata
brenda