EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.132 | -999 |
- |
more |
in phosphate buffer, enzyme shows Michaelis-Menten kinetics, in Tris buffer, enzyme shows marked cooperativity with respect to NAD+ binding. Phosphate and GMP are allosteric effectors |
654666 |
| 1.1.1.132 | 0.009 |
- |
GDP-D-mannose |
pH 8.0, 5°C, recombinant wild-type enzyme |
667316 |
| 1.1.1.132 | 0.0149 |
- |
GDP-D-mannose |
- |
285830 |
| 1.1.1.132 | 0.0149 |
- |
GDP-D-mannose |
24°C, pH 8.0 |
285830 |
| 1.1.1.132 | 0.017 |
- |
GDP-mannose |
- |
285829, 285831 |
| 1.1.1.132 | 0.023 |
- |
GDP-D-mannose |
pH 8.0, 5°C, recombinant mutant C213A |
667316 |
| 1.1.1.132 | 0.045 |
- |
GDP-D-mannose |
pH 8.0, 5°C, recombinant mutant C268A |
667316 |
| 1.1.1.132 | 0.084 |
- |
deoxy-GDP-D-mannose |
- |
285829, 285831 |
| 1.1.1.132 | 0.086 |
- |
NAD+ |
pH and temperature not specified in the publication |
725424 |
| 1.1.1.132 | 0.095 |
- |
GDP-D-mannose |
pH and temperature not specified in the publication |
725424 |
