EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.B38 | expression in Escherichia coli | Archaeoglobus fulgidus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.B38 | Mevinolin | competitive | Archaeoglobus fulgidus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.B38 | 0.16 | - |
NADH | pH 9.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 0.5 | - |
NADPH | pH 6.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 0.5 | - |
NAD+ | pH 10.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 0.62 | - |
mevalonate | 50°C, pH not specified in the publication | Archaeoglobus fulgidus | |
1.1.1.B38 | 1.7 | - |
NADP+ | pH 7.0, 50°C | Archaeoglobus fulgidus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.B38 | Archaeoglobus fulgidus | O28538 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.B38 | - |
Archaeoglobus fulgidus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.B38 | mevalonate + CoA + 2 NAD+ | optimal activity using NADP(H) occurs at pH from 1 to 3 units more acidic than that observed using NAD(H) | Archaeoglobus fulgidus | 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ | - |
r | |
1.1.1.B38 | mevalonate + CoA + 2 NADP+ | slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurs at a pH from 1 to 3 units more acidic than that observed using NAD(H) | Archaeoglobus fulgidus | 3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.B38 | AF1736 | - |
Archaeoglobus fulgidus |
1.1.1.B38 | HMG-CoA reductase | - |
Archaeoglobus fulgidus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.B38 | 85 | - |
- |
Archaeoglobus fulgidus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.B38 | 65 | 95 | 65°C: about 45% of maximal activity, 95°C: about 65% of maximal activity | Archaeoglobus fulgidus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.B38 | 0.08 | - |
NADH | pH 9.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 0.1 | - |
NAD+ | pH 10.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 2 | - |
NADPH | pH 6.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 6.8 | - |
NADP+ | pH 7.0, 50°C | Archaeoglobus fulgidus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.B38 | 6 | - |
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADPH | Archaeoglobus fulgidus |
1.1.1.B38 | 6.8 | - |
oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NADP+ | Archaeoglobus fulgidus |
1.1.1.B38 | 9 | - |
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADH | Archaeoglobus fulgidus |
1.1.1.B38 | 9.5 | 10 | oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NAD+ | Archaeoglobus fulgidus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.B38 | NAD+ | slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other | Archaeoglobus fulgidus | |
1.1.1.B38 | NADH | slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other | Archaeoglobus fulgidus | |
1.1.1.B38 | NADP+ | slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other | Archaeoglobus fulgidus | |
1.1.1.B38 | NADPH | slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other | Archaeoglobus fulgidus |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
1.1.1.B38 | 0.18 | - |
50°C, pH not specified in the publication | Archaeoglobus fulgidus | Mevinolin |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.B38 | 0.25 | - |
NADP+ | pH 7.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 1 | - |
NADPH | pH 6.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 2 | - |
NADH | pH 9.0, 50°C | Archaeoglobus fulgidus | |
1.1.1.B38 | 5 | - |
NAD+ | pH 10.0, 50°C | Archaeoglobus fulgidus |