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A structural basis for enantioselective inhibition of Candida rugosa lipase by long-chain aliphatic alcohols.
Molecular modeling showed that the enantiomers of heptyl 2-methyldecanoate are productively bound to the active site of Candida rugosa lipase in quite different conformations. The fast-reacting S-enantiomer may well occupy the previously identified acyl-binding tunnel in the active site of the lipas...
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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
1996
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143242/ https://ncbi.nlm.nih.gov/pubmed/8771199 |
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