EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.1.238 | synthesis | the enzyme can be a useful biocatalyst for the synthesis of simvastatin and other statin analogs. It is an attractive enzyme for engineered biosynthesis of pharmaceutically important cholesterol-lowering drugs | Aspergillus terreus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.238 | overexpression in Escherichia coli | Aspergillus terreus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.238 | S76A | no activity | Aspergillus terreus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.238 | monacolin J | competitive inhibitor of butyryl-CoA, substrate inhibition occurs due to binding of monacolin J to the free enzyme, forming a LovD-monacolin J complex and blocking entrance of butyryl-CoA | Aspergillus terreus | |
2.3.1.238 | additional information | no substrate inhibition by butyryl-CoA at high concentrations is observed | Aspergillus terreus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | additional information | - |
additional information | Km-value for hydrolysis of lovastain to monacolin J is 0.56 mM | Aspergillus terreus | |
2.3.1.238 | 1.59 | - |
butyryl-CoA | pH 7.9, 25°C | Aspergillus terreus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.238 | Aspergillus terreus | Q9Y7D1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.238 | - |
Aspergillus terreus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.238 | (S)-2-methylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J | - |
Aspergillus terreus | pravastatin + N-acetylcysteamine | - |
? | |
2.3.1.238 | (S)-2-methylbutanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | lovastatin + N-acetylcysteamine | - |
? | |
2.3.1.238 | alpha-dimethylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J | - |
Aspergillus terreus | huvastatin + N-acetylcysteamine | - |
? | |
2.3.1.238 | alpha-dimethylbutanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | simvastatin + N-acetylcysteamine | - |
? | |
2.3.1.238 | benzoyl-CoA + monacolin J | - |
Aspergillus terreus | ? + CoA | - |
? | |
2.3.1.238 | butanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | (1S,3R,7S,8S,8aR)-8-[2-[(2R,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl]ethyl]-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl butanoate + N-acetylcysteamine | - |
? | |
2.3.1.238 | butyryl-CoA + monacolin J | 87% conversion after 10 h | Aspergillus terreus | (1S,3R,7S,8S,8aR)-8-[2-[(2R,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl]ethyl]-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl butanoate + CoA | - |
? | |
2.3.1.238 | hexanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | ? + N-acetylcysteamine | - |
? | |
2.3.1.238 | additional information | the enzyme displays preference toward medium chain length (C3C6) acyl groups, with butyryl-CoA being the optimal alkylacyl-CoA substrate. Both acetyl- and octanoyl-CoA are poor substrates of LovD, with less than 10% acylation of monacolin J. The enzyme also catalyzes hydrolysis of lovastain to monacolin J. Butyryl-thioethane and butyryl-thioethanol are not competent substrates of the enzyme | Aspergillus terreus | ? | - |
? | |
2.3.1.238 | pentanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | ? + N-acetylcysteamine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.238 | LovD | - |
Aspergillus terreus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.238 | 25 | - |
assay at | Aspergillus terreus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | additional information | - |
additional information | kcat-value for hydrolysis of lovastain to monacolin J is 0.0035/s | Aspergillus terreus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.238 | 7.9 | - |
assay at | Aspergillus terreus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.238 | 0.33 | - |
monacolin J | pH 7.9, 25°C | Aspergillus terreus |