EC Number   |
KM Value [mM]  |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.88 | -999 |
- |
more |
kinetic analysis, overview. The enzyme exhibits positive cooperativity toward the substrates of the reductive reaction, but the oxidative reaction exhibits unusual double-saturation kinetics, distinctive among characterized HMG-CoA reductases. The unusual kinetics may arise from the presence of multiple active oligomeric states, each with different Vmax values |
740104 |
| 1.1.1.88 | 0.00734 |
- |
3-hydroxy-3-methylglutaryl-CoA |
at pH 7.4, temperature not specified in the publication |
760594 |
| 1.1.1.88 | 0.0285 |
- |
NADH |
at pH 7.4, temperature not specified in the publication |
760594 |
| 1.1.1.88 | 0.03 |
- |
CoASH |
H381A mutant, oxidative acylation of mevalonate |
287502 |
| 1.1.1.88 | 0.032 |
- |
NADH |
reductive deacylation to mevalonate |
287496, 287497 |
| 1.1.1.88 | 0.039 |
- |
CoA |
oxidative acylation of mevalonate |
287496, 287497 |
| 1.1.1.88 | 0.046 |
- |
CoA |
mevaldate oxidation |
287496, 287497 |
| 1.1.1.88 | 0.05 |
- |
CoASH |
oxidative acylation of mevalonate |
287499 |
| 1.1.1.88 | 0.05 |
- |
CoASH |
wild-type enzyme, oxidative acylation of mevalonate |
287502 |
| 1.1.1.88 | 0.05 |
- |
DL-3-hydroxy-3-methylglutaryl-CoA |
reductive deacylation to mevalonate |
287496, 287497 |
