Application | Comment | Organism |
---|---|---|
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 |
Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Aspergillus terreus |
Protein Variants | Comment | Organism |
---|---|---|
S76A | no activity | Aspergillus terreus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | |
additional information | no substrate inhibition by butyryl-CoA at high concentrations is observed | Aspergillus terreus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-value for hydrolysis of lovastain to monacolin J is 0.56 mM | Aspergillus terreus | |
1.59 | - |
butyryl-CoA | pH 7.9, 25°C | Aspergillus terreus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus terreus | Q9Y7D1 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Aspergillus terreus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-2-methylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J | - |
Aspergillus terreus | pravastatin + N-acetylcysteamine | - |
? | |
(S)-2-methylbutanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | lovastatin + N-acetylcysteamine | - |
? | |
alpha-dimethylbutanoyl-N-acetylcysteamine + 6-hydroxy-6-demethylmonacolin J | - |
Aspergillus terreus | huvastatin + N-acetylcysteamine | - |
? | |
alpha-dimethylbutanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | simvastatin + N-acetylcysteamine | - |
? | |
benzoyl-CoA + monacolin J | - |
Aspergillus terreus | ? + CoA | - |
? | |
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 | - |
? | |
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 | - |
? | |
hexanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | ? + N-acetylcysteamine | - |
? | |
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 | ? | - |
? | |
pentanoyl-N-acetylcysteamine + monacolin J | - |
Aspergillus terreus | ? + N-acetylcysteamine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LovD | - |
Aspergillus terreus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Aspergillus terreus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kcat-value for hydrolysis of lovastain to monacolin J is 0.0035/s | Aspergillus terreus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.9 | - |
assay at | Aspergillus terreus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.33 | - |
monacolin J | pH 7.9, 25°C | Aspergillus terreus |