EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.40 | (S)-malate + NAD(P)+ |
- |
Zea mays |
pyruvate + CO2 + NAD(P)H |
- |
? |
1.1.1.40 | (S)-malate + NAD(P)+ |
the unique and specialized C4-type enzyme has evolved fro the C3-type enzyme |
Zea mays |
pyruvate + CO2 + NAD(P)H |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
- |
Homo sapiens |
pyruvate + CO2 + NADH |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
- |
Homo sapiens |
pyruvate + CO2 + NADH |
- |
r |
1.1.1.40 | (S)-malate + NAD+ |
- |
Zea mays |
pyruvate + CO2 + NADH |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
at 39% of the activity with NADP+ |
Homo sapiens |
pyruvate + CO2 + NADH |
- |
ir |
1.1.1.40 | (S)-malate + NAD+ |
lower activity than with NADP+ |
Homo sapiens |
pyruvate + CO2 + NADH |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
NADP+ is preferred over NAD+ |
Saccharolobus solfataricus |
pyruvate + CO2 + NADH |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
low activity with NAD+ as cofactor |
Homo sapiens |
pyruvate + CO2 + NADH |
- |
? |
1.1.1.40 | (S)-malate + NAD+ |
when the R221G/K228R/I310V mutant is used with NADH, the mutant gives 1.2 and 2.7 times higher malate concentration than the wild-type with NADPH and NADH, respectively. These results can be partly explained by the alteration of the cofactor preference of the mutant enzyme, since the half-life of NADH is approximately 1.3times longer than that of NADPH at 50°C. However, the Km of the triple mutant for NAD+ remains 190times higher than that of the wild-type for NADP+ |
Thermococcus kodakarensis |
pyruvate + CO2 + NADH |
- |
r |