Protein Variants | Comment | Organism |
---|---|---|
D32A | activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 3% of the activity with NAD+ | Bacillus subtilis |
D32A/L187N | wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+ | Bacillus subtilis |
L187N | activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 7% of the activity with NAD+ | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.1 | - |
NAD+ | wild-type enzyme | Bacillus subtilis | |
0.5 | - |
NAD+ | mutant enzyme D32A | Bacillus subtilis | |
0.75 | - |
NAD+ | mutant enzyme D32A/L187N | Bacillus subtilis | |
1 | - |
NAD+ | mutant enzyme L187N | Bacillus subtilis | |
1.7 | - |
NADP+ | mutant enzyme D32A/L187N | Bacillus subtilis | |
7.1 | - |
NADP+ | mutant enzyme D32A and L187N | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Bacillus subtilis | glycolytic enzyme | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Bacillus subtilis | 3-phospho-D-glyceroyl phosphate + NADH | - |
? | |
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | glycolytic enzyme | Bacillus subtilis | 3-phospho-D-glyceroyl phosphate + NADH | - |
? | |
D-glyceraldehyde 3-phosphate + phosphate + NADP+ | - |
Bacillus subtilis | 3-phospho-D-glyceroyl phosphate + NADPH + H+ | - |
r | |
additional information | wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+ | Bacillus subtilis | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | - |
NADP+ | mutant enzyme D32A | Bacillus subtilis | |
2.5 | - |
NAD+ | mutant enzyme D32A/L187N | Bacillus subtilis | |
8 | - |
NADP+ | mutant enzyme L187N | Bacillus subtilis | |
17.7 | - |
NADP+ | mutant enzyme D32A/L187N | Bacillus subtilis | |
70 | - |
NAD+ | wild-type enzyme and mutant enzyme L187N | Bacillus subtilis | |
112 | - |
NAD+ | mutant enzyme L187N | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Bacillus subtilis | |
NADP+ | wild-type enzyme has no activity with NADP+. The mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+. Activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme. Activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme. Mutant enzymes D32A and L187N also show activity with NADP+, 3-7% of the activity with NAD+ | Bacillus subtilis |