EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.238 | S76A | active site mutant, no activity | Aspergillus terreus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | 0.039 | - |
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | pH and temperature not specified in the publication | Aspergillus terreus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.238 | monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | Aspergillus terreus | the enzyme is involved in lovastatin biosynthesis | lovastatin acid + [2-methylbutanoate polyketide synthase] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.238 | Aspergillus terreus | Q9Y7D1 | - |
- |
2.3.1.244 | Aspergillus terreus | Q9Y7D5 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.238 | monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | the enzyme is involved in lovastatin biosynthesis | Aspergillus terreus | lovastatin acid + [2-methylbutanoate polyketide synthase] | - |
? | |
2.3.1.238 | monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | the enzyme primarily interacts with the ACP domain of 2-methylbutanoate polyketide synthase (LovF) and the protein-protein interactions leads to highly efficient transfer of the diketide product | Aspergillus terreus | lovastatin acid + [2-methylbutanoate polyketide synthase] | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.238 | LovD | - |
Aspergillus terreus |
2.3.1.244 | lovastatin diketide synthase | - |
Aspergillus terreus |
2.3.1.244 | LovF | - |
Aspergillus terreus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | 0.806 | - |
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | pH and temperature not specified in the publication | Aspergillus terreus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.238 | physiological function | the enzyme is involved in lovastatin biosynthesis | Aspergillus terreus |
2.3.1.244 | physiological function | enzyme LovF synthesizes the alpha-S-methylbutyrate side chain that is subsequently transferred to monacolin J to yield the cholesterol-lowering natural product lovastatin. The diketide product of LovF is offloaded from the LovF acyl carrier protein domain by the dissociated acyltransferase LovD. LovD primarily interacts with the acyl carrier protein domain of LovF and the protein-protein interactions lead to highly efficient transfer of the diketide product. The catalytic efficiency is enhanced nearly one millionfold when LovF is used as the acyl carrier instead of N-acetylcysteamine | Aspergillus terreus |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | 20.7 | - |
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] | pH and temperature not specified in the publication | Aspergillus terreus |