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beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
D-galacturonate + NADP+
L-galactono-1,4-lactone + NADPH + H+
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonic acid + D-xylose
mucic acid + ?
D-galacturonic acid + lactose
mucic acid + ?
D-galacturonic acid + NAD+
D-galactaric acid + NADH + H+
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
D-galacturonic acid + NADPH
L-galactonate + NADP+
-
-
-
-
?
D-glucuronate + NAD+
D-glucaric acid 3,6-lactone + NADH + H+
-
weak reversible reaction, 3% of the activity compared to the forward reaction
-
r
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
D-glucuronic acid + NADH
L-gulonic acid + NAD+
-
-
-
-
?
D-glucuronic acid + NADPH
L-gulonic acid + NADP+
-
-
-
-
?
D-glucuronic acid from a beechwood xylan + NAD+
D-glucaric acid + NADH + H+
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone + NADP+
-
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
L-galactonate + NADP+
D-galacturonic acid + NADPH
-
-
-
-
?
L-galactono-1,4-lactone + NADPH
?
-
-
-
-
?
L-gulonic acid + NAD+
D-glucuronic acid + NADH
-
-
-
-
?
L-gulono-1,4-lactone + NADPH
?
-
-
-
-
?
additional information
?
-
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
50% of the activity compared to D-glucoronate
-
ir
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonic acid + D-xylose
mucic acid + ?
-
-
-
-
?
D-galacturonic acid + D-xylose
mucic acid + ?
-
-
-
-
?
D-galacturonic acid + lactose
mucic acid + ?
-
-
-
-
?
D-galacturonic acid + lactose
mucic acid + ?
-
-
-
-
?
D-galacturonic acid + NAD+
D-galactaric acid + NADH + H+
-
-
-
?
D-galacturonic acid + NAD+
D-galactaric acid + NADH + H+
-
-
-
?
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
ir
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
strong substrate specificity, best substrate
-
ir
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
inclusion of a third enzyme, Udh, apart from myo-inositol-1-phosphate synthase (Ino1) from Saccharomyces cerevisiae and myo-inositol oxygenase (MIOX) from mice, facilitates conversion of D-glucuronate to D-glucaric acid. Up to 1 g/l of glucaric acid is produced with the three enzymes, whereas only 0.27 g/l of glucuronic acid is produced in the system harboring the two genes of INO1 and MIOX. Udh activity is highest, more than 2fold higher than Ino1 activity and 3fold higher than MIOX activity. The high activity of Udh may pull glucose flux through the glucaric acid pathway, leading to a relatively higher titer of glucaric acid
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
inclusion of a third enzyme, Udh, apart from myo-inositol-1-phosphate synthase (Ino1) from Saccharomyces cerevisiae and myo-inositol oxygenase (MIOX) from mice, facilitates conversion of D-glucuronate to D-glucaric acid. Up to 1 g/l of glucaric acid is produced with the three enzymes, whereas only 0.27 g/l of glucuronic acid is produced in the system harboring the two genes of INO1 and MIOX. Udh activity is highest, more than 2fold higher than Ino1 activity and 3fold higher than MIOX activity. The high activity of Udh may pull glucose flux through the glucaric acid pathway, leading to a relatively higher titer of glucaric acid
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
assay at pH 8.0
-
-
?
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
assay at pH 8.0
-
-
?
D-glucuronic acid from a beechwood xylan + NAD+
D-glucaric acid + NADH + H+
after 60 min of incubation at 50°C, the enzyme exhibits a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from beechwood xylans formed by xylanase and alpha-glucuronidase
-
-
?
D-glucuronic acid from a beechwood xylan + NAD+
D-glucaric acid + NADH + H+
after 60 min of incubation at 50°C, the enzyme exhibits a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from beechwood xylans formed by xylanase and alpha-glucuronidase
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
-
?
D-mannuronate + NAD+
? + NADH + H+
-
-
-
-
?
additional information
?
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
D-galacturonic acid + NADPH
L-galactonate + NADP+
-
-
-
-
?
D-glucuronate + NAD+
D-glucaric acid 3,6-lactone + NADH + H+
-
weak reversible reaction, 3% of the activity compared to the forward reaction
-
r
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
D-glucuronic acid + NADPH
L-gulonic acid + NADP+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
-
50% of the activity compared to D-glucoronate
-
ir
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-galacturonic acid + NAD+ + H2O
D-galactaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
ir
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
-
strong substrate specificity, best substrate
-
ir
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.02 - 628
beta-D-galacturonate
0.14 - 465
beta-D-glucuronate
0.04 - 0.16
D-galacturonate
0.115 - 3.15
D-galacturonic acid
0.15 - 0.37
D-glucuronate
0.15 - 6.3
D-glucuronic acid
0.165
D-glucuronic acid from a beechwood xylan
at pH 7.0 and 60°C
-
7.1
D-glucurono-3,6-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
3.3
L-galactonate
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
8.1
L-galactono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
4.7
L-Gulonic acid
-
with NADP+ as cosubstrate, at pH 7.5 and 25°C
9.5
L-gulono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.4
NADH
-
at pH 7.5 and 25°C
0.006
NADPH
-
with D-glucuronic acid as cosubstrate, at pH 7.5 and 25°C
additional information
additional information
-
0.02
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.03
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.03
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.04
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.053
beta-D-galacturonate
-
pH 8.0, 25°C, method A
0.1
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.106
beta-D-galacturonate
-
pH 8.0, 25°C
0.107
beta-D-galacturonate
pH 8.0, 25°C
0.13
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
0.138
beta-D-galacturonate
-
pH 8.0, 25°C, method B
0.14
beta-D-galacturonate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
0.148
beta-D-galacturonate
-
pH 8.0, 25°C, method A
0.15
beta-D-galacturonate
mutant enzyme T113V, at pH 8.0 and 25°C
0.16
beta-D-galacturonate
-
pH 8.0, 25°C
0.16
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
wild type enzyme, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
mutant enzyme A172V, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
mutant enzyme D246N, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
mutant enzyme M175I, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
0.18
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
0.19
beta-D-galacturonate
mutant enzyme Q55R, at pH 8.0 and 25°C
0.19
beta-D-galacturonate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
0.2
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.2
beta-D-galacturonate
mutant enzyme I88L, at pH 8.0 and 25°C
0.21
beta-D-galacturonate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
0.22
beta-D-galacturonate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
0.22
beta-D-galacturonate
mutant enzyme Y116F, at pH 8.0 and 25°C
0.279
beta-D-galacturonate
-
pH 8.0, 25°C, method B
0.3
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.41
beta-D-galacturonate
mutant enzyme I114T, at pH 8.0 and 25°C
55
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
64
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
628
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.14
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.2
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.2
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.3
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.3
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.43
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
0.48
beta-D-glucuronate
-
pH 8.0, 25°C, method A
0.5
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.65
beta-D-glucuronate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
0.69
beta-D-glucuronate
-
pH 8.0, 25°C
0.7
beta-D-glucuronate
-
wild type enzyme, at pH 8.0 and 25°C
0.9
beta-D-glucuronate
-
mutant enzyme A41P/H101N/H236K, at pH 8.0 and 25°C
0.9
beta-D-glucuronate
-
mutant enzyme A41P/H101Y/H236K, at pH 8.0 and 25°C
0.9
beta-D-glucuronate
-
mutant enzyme H101N/H236K, at pH 8.0 and 25°C
0.9
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
0.95
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
1
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
1
beta-D-glucuronate
-
mutant enzyme A41P/H101N/H236R, at pH 8.0 and 25°C
1
beta-D-glucuronate
-
mutant enzyme A41P/H101Y/H236R, at pH 8.0 and 25°C
1
beta-D-glucuronate
-
mutant enzyme H101Y/H236K, at pH 8.0 and 25°C
1.03
beta-D-glucuronate
mutant enzyme M175I, at pH 8.0 and 25°C
1.08
beta-D-glucuronate
-
pH 8.0, 25°C, method B
1.1
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
1.1
beta-D-glucuronate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
1.2
beta-D-glucuronate
-
mutant enzyme A41P/H236K, at pH 8.0 and 25°C
1.2
beta-D-glucuronate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
1.27
beta-D-glucuronate
-
pH 8.0, 25°C
1.3
beta-D-glucuronate
-
pH 8.0, 25°C, method A
1.3
beta-D-glucuronate
mutant enzyme D246N, at pH 8.0 and 25°C
1.3
beta-D-glucuronate
-
mutant enzyme H236K, at pH 8.0 and 25°C
1.34
beta-D-glucuronate
pH 8.0, 25°C
1.5
beta-D-glucuronate
mutant enzyme I88L, at pH 8.0 and 25°C
1.5
beta-D-glucuronate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
1.6
beta-D-glucuronate
wild type enzyme, at pH 8.0 and 25°C
1.7
beta-D-glucuronate
mutant enzyme A172V, at pH 8.0 and 25°C
1.7
beta-D-glucuronate
mutant enzyme Q55R, at pH 8.0 and 25°C
1.7
beta-D-glucuronate
mutant enzyme T113V, at pH 8.0 and 25°C
1.94
beta-D-glucuronate
-
pH 8.0, 25°C, method B
2
beta-D-glucuronate
mutant enzyme Y116F, at pH 8.0 and 25°C
3.2
beta-D-glucuronate
mutant enzyme I114T, at pH 8.0 and 25°C
59
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
64
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
465
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.04
D-galacturonate
-
0.054
D-galacturonate
-
-
0.057
D-galacturonate
-
-
0.115
D-galacturonic acid
at pH 7.0 and 60°C
0.95
D-galacturonic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
3.15
D-galacturonic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
0.15
D-glucuronate
-
-
0.15
D-glucuronic acid
-
mutant enzyme A39P/H99Y/H234K, at pH 8.0 and 30°C
0.17
D-glucuronic acid
-
mutant enzyme H99Y/H234K, at pH 8.0 and 30°C
0.18
D-glucuronic acid
-
mutant enzyme A39P/H234K, at pH 8.0 and 30°C
0.2
D-glucuronic acid
-
wild type enzyme, at pH 8.0 and 30°C
0.2
D-glucuronic acid
-
mutant enzyme A39P/H99Y, at pH 8.0 and 30°C
0.23
D-glucuronic acid
-
mutant enzyme H99Y, at pH 8.0 and 30°C
0.24
D-glucuronic acid
-
mutant enzyme H234K, at pH 8.0 and 30°C
0.26
D-glucuronic acid
-
mutant enzyme A39P, at pH 8.0 and 30°C
3.34
D-glucuronic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
6.3
D-glucuronic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
6.4
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
7.3
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
8.3
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
9
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
9.5
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
13.6
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
19.4
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
22.05
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
112
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
142
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.06
NAD+
-
pH 8.0, 25°C, method B
0.078
NAD+
-
pH 8.0, 25°C, method B
0.1
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.1
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.115
NAD+
at pH 7.0 and 60°C
0.2
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.2
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.25
NAD+
-
pH 8.0, 25°C, method A
0.4
NAD+
-
pH 8.0, 25°C, method A
0.4
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
5.3
NAD+
-
with 0.67 mM D-galacturonate
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics
-
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics
-
additional information
additional information
Michaelis-Menten kinetics and thermodynamics
-
additional information
additional information
-
steady-state and stopped-flow kinetics, Michaelis-Menten kinetics, and thermodynamics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 - 76
beta-D-galacturonate
6 - 333
beta-D-glucuronate
0.24 - 26.7
D-galacturonate
13.6 - 58.333
D-galacturonic acid
7.6 - 380
D-glucuronic acid
65.882
D-glucuronic acid from a beechwood xylan
at pH 7.0 and 60°C
-
2.3
D-glucurono-3,6-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.75
L-galactonate
-
with NADP+ as cosubstrate, at pH 7.5 and 25°C
0.41
L-galactono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.97
L-Gulonic acid
-
with NADP+ as cosubstrate, at pH 7.5 and 25°C
0.41
L-gulono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
7.4
NADH
-
at pH 7.5 and 25°C
9.6
NADPH
-
with D-glucuronic acid as cosubstrate, at pH 7.5 and 25°C
2 - 8
beta-D-galacturonate
mutant enzyme Q55R, at pH 8.0 and 25°C
3
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
4
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
10
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
13
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
15.3
beta-D-galacturonate
-
pH 8.0, 25°C
17
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
17
beta-D-galacturonate
mutant enzyme I114T, at pH 8.0 and 25°C
17
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
17
beta-D-galacturonate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
17.1
beta-D-galacturonate
-
pH 8.0, 25°C
17.4
beta-D-galacturonate
-
pH 8.0, 25°C, method A
17.9
beta-D-galacturonate
-
pH 8.0, 25°C, method B
19
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
20
beta-D-galacturonate
mutant enzyme M175I, at pH 8.0 and 25°C
20
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
20
beta-D-galacturonate
mutant enzyme T113V, at pH 8.0 and 25°C
21
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
22
beta-D-galacturonate
mutant enzyme D246N, at pH 8.0 and 25°C
22
beta-D-galacturonate
mutant enzyme I88L, at pH 8.0 and 25°C
22
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
23
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
25
beta-D-galacturonate
mutant enzyme Y116F, at pH 8.0 and 25°C
27
beta-D-galacturonate
mutant enzyme A172V, at pH 8.0 and 25°C
27
beta-D-galacturonate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
27.8
beta-D-galacturonate
pH 8.0, 25°C
29
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
29
beta-D-galacturonate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
30
beta-D-galacturonate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
30.8
beta-D-galacturonate
wild type enzyme, at pH 8.0 and 25°C
33.8
beta-D-galacturonate
-
pH 8.0, 25°C, method A
51.6
beta-D-galacturonate
-
pH 8.0, 25°C, method B
59
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
76
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
6
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
7
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
50
beta-D-glucuronate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
53
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
58
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
59
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
63
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
75
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
82
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
101
beta-D-glucuronate
-
pH 8.0, 25°C, method B
108
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
119
beta-D-glucuronate
-
pH 8.0, 25°C
119
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
130
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
142
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
152
beta-D-glucuronate
-
pH 8.0, 25°C
153
beta-D-glucuronate
mutant enzyme M175I, at pH 8.0 and 25°C
155
beta-D-glucuronate
mutant enzyme I114T, at pH 8.0 and 25°C
159
beta-D-glucuronate
-
pH 8.0, 25°C, method A
171
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
179
beta-D-glucuronate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
192
beta-D-glucuronate
mutant enzyme D246N, at pH 8.0 and 25°C
192
beta-D-glucuronate
mutant enzyme I88L, at pH 8.0 and 25°C
192
beta-D-glucuronate
mutant enzyme T113V, at pH 8.0 and 25°C
200
beta-D-glucuronate
mutant enzyme Y116F, at pH 8.0 and 25°C
212
beta-D-glucuronate
-
pH 8.0, 25°C, method B
214
beta-D-glucuronate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
217
beta-D-glucuronate
pH 8.0, 25°C
219
beta-D-glucuronate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
225
beta-D-glucuronate
mutant enzyme A172V, at pH 8.0 and 25°C
263
beta-D-glucuronate
wild type enzyme, at pH 8.0 and 25°C
270
beta-D-glucuronate
mutant enzyme Q55R, at pH 8.0 and 25°C
274
beta-D-glucuronate
-
pH 8.0, 25°C, method A
333
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.24
D-galacturonate
-
13.6
D-galacturonic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
18.5
D-galacturonic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
58.333
D-galacturonic acid
at pH 7.0 and 60°C
0.55
D-glucuronate
-
7.6
D-glucuronic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
13
D-glucuronic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
161
D-glucuronic acid
-
wild type enzyme, at pH 8.0 and 30°C
179
D-glucuronic acid
-
mutant enzyme H99Y, at pH 8.0 and 30°C
192
D-glucuronic acid
-
mutant enzyme A39P, at pH 8.0 and 30°C
195
D-glucuronic acid
-
mutant enzyme H234K, at pH 8.0 and 30°C
239
D-glucuronic acid
-
mutant enzyme A39P/H99Y, at pH 8.0 and 30°C
295
D-glucuronic acid
-
mutant enzyme A39P/H234K, at pH 8.0 and 30°C
318
D-glucuronic acid
-
mutant enzyme H99Y/H234K, at pH 8.0 and 30°C
380
D-glucuronic acid
-
mutant enzyme A39P/H99Y/H234K, at pH 8.0 and 30°C
3.4
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
4
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
6.4
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
7
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
8
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
9
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
78
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
85
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
92
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
107
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
7
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
62
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
74.667
NAD+
at pH 7.0 and 60°C
113
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
144
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
215
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.04 - 794
beta-D-galacturonate
0.1 - 829
beta-D-glucuronate
5.87 - 509.018
D-galacturonic acid
1.2 - 910
D-glucuronic acid
400.014
D-glucuronic acid from a beechwood xylan
at pH 7.0 and 60°C
-
0.32
D-glucurono-3,6-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.23
L-galactonate
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.05
L-galactono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
0.2
L-Gulonic acid
-
with NADP+ as cosubstrate, at pH 7.5 and 25°C
0.04
L-gulono-1,4-lactone
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
19
NADH
-
at pH 7.5 and 25°C
1655
NADPH
-
with D-glucuronic acid as cosubstrate, at pH 7.5 and 25°C
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics
-
0.04
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.07
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
41
beta-D-galacturonate
mutant enzyme I114T, at pH 8.0 and 25°C
78
beta-D-galacturonate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
88
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
96
beta-D-galacturonate
-
pH 8.0, 25°C
98
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
104
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
111
beta-D-galacturonate
mutant enzyme Y116F, at pH 8.0 and 25°C
112
beta-D-galacturonate
mutant enzyme I88L, at pH 8.0 and 25°C
116
beta-D-galacturonate
mutant enzyme M175I, at pH 8.0 and 25°C
125
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
125
beta-D-galacturonate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
126
beta-D-galacturonate
mutant enzyme D246N, at pH 8.0 and 25°C
126
beta-D-galacturonate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
130
beta-D-galacturonate
-
pH 8.0, 25°C, method B
132
beta-D-galacturonate
mutant enzyme T113V, at pH 8.0 and 25°C
138
beta-D-galacturonate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
151
beta-D-galacturonate
mutant enzyme A172V, at pH 8.0 and 25°C
152
beta-D-galacturonate
mutant enzyme Q55R, at pH 8.0 and 25°C
155
beta-D-galacturonate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
161
beta-D-galacturonate
-
pH 8.0, 25°C
172
beta-D-galacturonate
wild type enzyme, at pH 8.0 and 25°C
185
beta-D-galacturonate
-
pH 8.0, 25°C, method B
187
beta-D-galacturonate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
200
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
228
beta-D-galacturonate
-
pH 8.0, 25°C, method A
260
beta-D-galacturonate
pH 8.0, 25°C
328
beta-D-galacturonate
-
pH 8.0, 25°C, method A
406
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
430
beta-D-galacturonate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
628
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
646
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
794
beta-D-galacturonate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.1
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.11
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
48
beta-D-glucuronate
mutant enzyme I114T, at pH 8.0 and 25°C
77
beta-D-glucuronate
mutant enzyme Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N, at pH 8.0 and 25°C
93.5
beta-D-glucuronate
-
pH 8.0, 25°C, method B
93.7
beta-D-glucuronate
-
pH 8.0, 25°C
97.5
beta-D-glucuronate
-
mutant enzyme H236K, at pH 8.0 and 25°C
101
beta-D-glucuronate
mutant enzyme Y116F, at pH 8.0 and 25°C
109
beta-D-glucuronate
-
pH 8.0, 25°C, method B
111
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C
115
beta-D-glucuronate
mutant enzyme T113V, at pH 8.0 and 25°C
116.7
beta-D-glucuronate
-
mutant enzyme H101Y/H236K, at pH 8.0 and 25°C
125
beta-D-glucuronate
mutant enzyme I88L, at pH 8.0 and 25°C
136
beta-D-glucuronate
mutant enzyme A172V, at pH 8.0 and 25°C
136
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
138
beta-D-glucuronate
mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C
139
beta-D-glucuronate
mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C
139.7
beta-D-glucuronate
-
mutant enzyme H101N/H236K, at pH 8.0 and 25°C
146
beta-D-glucuronate
mutant enzyme D246N, at pH 8.0 and 25°C
149
beta-D-glucuronate
mutant enzyme M175I, at pH 8.0 and 25°C
149.7
beta-D-glucuronate
-
mutant enzyme A41P/H101N/H236K, at pH 8.0 and 25°C
160.5
beta-D-glucuronate
-
mutant enzyme A41P/H101Y/H236R, at pH 8.0 and 25°C
161
beta-D-glucuronate
wild type enzyme, at pH 8.0 and 25°C
161
beta-D-glucuronate
mutant enzyme Q55R, at pH 8.0 and 25°C
162
beta-D-glucuronate
pH 8.0, 25°C
162
beta-D-glucuronate
mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C
164
beta-D-glucuronate
mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C
167.3
beta-D-glucuronate
-
mutant enzyme A41P/H101Y/H236K, at pH 8.0 and 25°C
170
beta-D-glucuronate
-
mutant enzyme A41P/H101N/H236R, at pH 8.0 and 25°C
179.5
beta-D-glucuronate
-
mutant enzyme A41P/H236K, at pH 8.0 and 25°C
186
beta-D-glucuronate
mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C
201
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
210
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
211
beta-D-glucuronate
-
pH 8.0, 25°C, method A
220
beta-D-glucuronate
-
pH 8.0, 25°C
257
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
269
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
274
beta-D-glucuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
286.4
beta-D-glucuronate
-
wild type enzyme, at pH 8.0 and 25°C
331
beta-D-glucuronate
-
pH 8.0, 25°C, method A
342
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
465
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
829
beta-D-glucuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
5.87
D-galacturonic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
14.3
D-galacturonic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
509.018
D-galacturonic acid
at pH 7.0 and 60°C
1.2
D-glucuronic acid
-
with NADH as cosubstrate, at pH 7.5 and 25°C
3.89
D-glucuronic acid
-
with NADPH as cosubstrate, at pH 7.5 and 25°C
720
D-glucuronic acid
-
mutant enzyme A39P/H99Y, at pH 8.0 and 30°C
730
D-glucuronic acid
-
mutant enzyme A39P, at pH 8.0 and 30°C
770
D-glucuronic acid
-
mutant enzyme H99Y, at pH 8.0 and 30°C
800
D-glucuronic acid
-
wild type enzyme, at pH 8.0 and 30°C
810
D-glucuronic acid
-
mutant enzyme H234K, at pH 8.0 and 30°C
840
D-glucuronic acid
-
mutant enzyme A39P/H234K, at pH 8.0 and 30°C
860
D-glucuronic acid
-
mutant enzyme H99Y/H234K, at pH 8.0 and 30°C
910
D-glucuronic acid
-
mutant enzyme A39P/H99Y/H234K, at pH 8.0 and 30°C
0.03
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.03
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
0.3
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.7
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
0.7
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
4
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
9
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
11
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
11
D-Mannuronate
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
12
D-Mannuronate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer
622.22
NAD+
at pH 7.0 and 60°C
638
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
785
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
1083
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
1262
NAD+
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
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physiological function
-
ascorbate accumulation is affected mainly by biosynthesis rather than recycling in radish root, and the L-galactose pathway may be the major biosynthetic route of ascorbate, and moreover, the salvage pathway may also contribute to ascorbate accumulation. Ascorbate level regulation involves the D-galacturonate reductase and GDP-D-mannose diphosphorylase
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
-
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
-
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
-
uronate dehydrogenases catalyses the initial step in an oxidative pathway
metabolism
-
the enzyme is proposed to be part of the salvage pathway in ascorbate production as galacturonate acid reductase, GalUR, EC 1.1.1.203, converting D-galacturonate to L-galactono-1,4-lactone, ascorbate biosynthesis and recycling pathways in plants, overview
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
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A39P
-
the mutant shows 103.5% activity compared to the wild type enzyme
A39P/H234K
-
the mutant shows 165.7% activity compared to the wild type enzyme
A39P/H99Y
-
the mutant shows 146.8% activity compared to the wild type enzyme
A39P/H99Y/H234K
-
the triple mutant shows 247.6% activity compared to the wild type enzyme, a 400fold improvement in half-life at 59°C, and a 5°C improvement in T50 (10 min) value
A41P/H101N/H236K
-
the mutant shows 52.3% catalytic efficiency as compared to the wild type enzyme
A41P/H101N/H236R
-
the mutant shows 59.3% catalytic efficiency as compared to the wild type enzyme
A41P/H101Y/H236K
-
the mutant shows 58.4% catalytic efficiency, higher kinetic and thermodynamic stability with a T50 value of 62.2°C after 15 min (3.2°C improvement) as compared to the wild type enzyme
A41P/H101Y/H236R
-
the mutant shows 56% catalytic efficiency as compared to the wild type enzyme
A41P/H236K
-
the mutant shows 62.7% catalytic efficiency as compared to the wild type enzyme
D34S
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
H101N/H236K
-
the mutant shows 48.8% catalytic efficiency as compared to the wild type enzyme
H101Y/H236K
-
the mutant shows 40.8% catalytic efficiency as compared to the wild type enzyme
H234K
-
the mutant shows 129.4% activity compared to the wild type enzyme
H236K
-
the mutant shows 34% catalytic efficiency as compared to the wild type enzyme
H99Y
-
the mutant shows 109.6% activity compared to the wild type enzyme
H99Y/H234K
-
the mutant shows 175.4% activity compared to the wild type enzyme
N112E
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
Q14F
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
S165E
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
S36L
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
S75T
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
Y136A
inactive. Crystal structure shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
D34S
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
N112E
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
Q14F
-
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
-
S165E
-
the mutant shows a high selectivity of D-galacturonic acid and its substrate intermediates for D-galactaric acid production
-
S75T
-
the mutant shows a high binding affinity to D-glucuronic acid and its substrate intermediates such as D-glucaro-1,4-lactone and D-glucaro-1,5-lactone. The mutant exhibits a low binding affinity to the substrate and cofactor required for D-galactaric acid production
-
Y136A
-
inactive. Crystal structure shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
-
A39P
-
the mutant shows 103.5% activity compared to the wild type enzyme
-
A39P/H99Y
-
the mutant shows 146.8% activity compared to the wild type enzyme
-
A39P/H99Y/H234K
-
the triple mutant shows 247.6% activity compared to the wild type enzyme, a 400fold improvement in half-life at 59°C, and a 5°C improvement in T50 (10 min) value
-
H234K
-
the mutant shows 129.4% activity compared to the wild type enzyme
-
H99Y
-
the mutant shows 109.6% activity compared to the wild type enzyme
-
A172V
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
I114T
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
I88L
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
L158A/N159C/I160V
the mutant shows increased catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
M175I
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
N99K/L100H/K102V/P103K/I105V
the mutant shows wild type activity with beta-D-glucuronate and reduced catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
Q55R
the mutant shows wild type activity with beta-D-glucuronate and reduced catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
Q55R/I88L/N99K/L100H/K102V/P103K/I105V/T113V/I114T/Y116F/L158A/N159C/I160V/A172V/M175I/D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/D246N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/M175I
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/A172V/M175I/D236N
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
T113V/M175I/D246N
the mutant shows increased catalytic efficiency with beta-D-glucuronate and decreased catalytic efficiency with beta-D-galacturonate compared to the wild type enzyme
Y116F
the mutant shows reduced catalytic efficiency with beta-D-glucuronate and beta-D-galacturonate compared to the wild type enzyme
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Bateman, D.F.; Kosuge, T.; Kilgore, W.W.
Purification and properties of uronate dehydrogenase from Pseudomonas syringae
Arch. Biochem. Biophys.
136
97-105
1970
Pseudomonas syringae
brenda
Wagner, G.; Hollmann, S.
Uronic acid dehydrogenase from Pseudomonas syringae. Purification and properties
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