EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
1.1.1.39 | -999 |
- |
more |
- |
286703, 286719 |
1.1.1.39 | -999 |
- |
more |
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 |
741121 |
1.1.1.39 | -999 |
- |
more |
detailed kinetic mechanism study, steady-state kinetics |
654720 |
1.1.1.39 | -999 |
- |
more |
kinetic analysis and comparison of the different isozymes MAD-ME1, NAD-ME2, and NAD-MEH, and of mutants NADME1q and NAD-ME2q, overview |
712417 |
1.1.1.39 | -999 |
- |
more |
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 |
711147 |
1.1.1.39 | -999 |
- |
more |
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 |
711147 |
1.1.1.39 | -999 |
- |
more |
kinetics |
654623 |
1.1.1.39 | -999 |
- |
more |
kinetics analysis of isozymes ME2 and ME3 |
712942 |
1.1.1.39 | -999 |
- |
more |
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 |
685123 |
1.1.1.39 | -999 |
- |
more |
Michaelis-Menten kinetics |
741191 |