Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CuSO4 | 50.7% inhibition by 1 mM, 96.3% inhibition by 20 mM, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme | Mycobacterium tuberculosis | |
Zn2+ | 26.5% inhibition by 1 mM ZnCl2, 90.1% inhibition by 20 mM ZnCl2, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0982 | - |
NADH | - |
Mycobacterium tuberculosis | |
0.31 | - |
NAD+ | - |
Mycobacterium tuberculosis | |
1.45 | - |
pyruvate | - |
Mycobacterium tuberculosis | |
13.8 | - |
L-Ala | - |
Mycobacterium tuberculosis | |
35.4 | - |
NH4+ | - |
Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Ala + H2O + NAD+ | Mycobacterium tuberculosis | since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala | pyruvate + NH3 + NADH | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+ | oxidative deamination proceeds by an random-ordered mechanism | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-2-aminobutanoate + H2O + NAD+ | in the reverse reaction 2-oxobutanoate reacts with 1.2% of the activity with pyruvate | Mycobacterium tuberculosis | 2-oxobutanoate + NH3 + NADH + H+ | - |
r | |
L-2-aminobutanoate + H2O + NAD+ | 0.7% of the activity with L-Ala | Mycobacterium tuberculosis | 2-oxobutanoate + NH3 + NADH + H+ | - |
r | |
L-Ala + H2O + NAD+ | - |
Mycobacterium tuberculosis | pyruvate + NH3 + NADH | - |
r | |
L-Ala + H2O + NAD+ | since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala | Mycobacterium tuberculosis | pyruvate + NH3 + NADH | - |
? | |
L-Ala + H2O + NADP+ | in the reverse direction NADPH reacts at 1.6% of the activity with NADH | Mycobacterium tuberculosis | pyruvate + NH3 + NADPH | - |
r | |
L-Ala + H2O + NADP+ | 2.5% of the activity with NAD+ | Mycobacterium tuberculosis | pyruvate + NH3 + NADPH | - |
r | |
L-Ser + H2O + NAD+ | no activity | Mycobacterium tuberculosis | 3-hydroxypyruvate + NH3 + NADH | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
4 h, 25% loss of activity, recombinant enzyme | Mycobacterium tuberculosis |
65.7 | - |
5 min, 50% loss of activity, recombinant enzyme | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 7.5 | reductive amination | Mycobacterium tuberculosis |
10 | 11 | oxidative deamination | Mycobacterium tuberculosis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | pH 6.0: about 30% of maximal activity, pH 8.5: about 25% of maximal activity, reductive amination | Mycobacterium tuberculosis |
8.5 | 11.5 | pH 8.5: about 35% of maximal activity, pH 11.5: about 20% of maximal activity, oxidative deamination | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Mycobacterium tuberculosis | |
NADH | - |
Mycobacterium tuberculosis | |
NADP+ | - |
Mycobacterium tuberculosis | |
NADPH | - |
Mycobacterium tuberculosis |