EC Number |
Cofactor |
Reference |
---|
1.1.1.88 | more |
sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, overview |
723092 |
1.1.1.88 | more |
sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, specificity-determining residue of HMGR from Pseudomonas mevalonii is D646, overview |
723092 |
1.1.1.88 | more |
the enzyme prefers NAD(H) over NADP(H) as a cofactor, suggesting an oxidative physiological role for the enzyme |
740104 |
1.1.1.88 | more |
very detailed kinetic studies of mutants concerning NAD+/NADP+-affinities, the best specificity improvement is achieved by the D146A/L148R-mutant |
287505 |
1.1.1.88 | NAD+ |
- |
287495, 287496, 287497, 287498, 287499, 287501, 287502, 287504, 287505, 287506, 287507, 287508, 654225, 657303, 723092, 740104, 760603, 761344 |
1.1.1.88 | NAD+ |
four-electron pyridine oxidoreductase |
287500 |
1.1.1.88 | NADH |
- |
654225, 656615, 657303, 723092, 740104 |
1.1.1.88 | NADH |
NADH-specific enzyme |
760594 |
1.1.1.88 | NADH |
reverse reaction |
287495, 287496, 287497, 287498, 287499, 287500, 287501, 287502, 287504, 287505, 287506, 287507, 287508 |
1.1.1.88 | NADP+ |
NAD+ is 600000fold more efficient than NADP+ in wild-type enzyme |
287505 |