Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-