Semiempirical molecular orbital studies of the acylation step in the lipase-catalyzed ester hydrolysis

Jian Hua Zhao, Hsuan Liang Liu, Hsin Yi Lin, Chih Hung Huang, Hsu Wei Fang, Shau Wei Tsai

Research output: Contribution to journalArticle


In this study, we present the results from the semiempirical molecular orbital calculations for the acylation step in the lipase-catalyzed ester hydrolysis. The results reveal that the lowest energy path for the formation of the tetrahedral intermediate is for the serine residue of the catalytic triad to attack the substrate, followed by coupling heavy atom movement and proton transfer. The calculations of four active site models show that the cooperation of the aspartate group and the oxyanion hole is capable of lowering the activation energy by about 16 kcalmol-1. Our results further suggest that the lipase-catalyzed ester hydrolysis adopts the single proton transfer mechanism.

Original languageEnglish
Pages (from-to)835-842
Number of pages8
JournalJournal of the Chinese Chemical Society
Issue number4
Publication statusPublished - Jan 1 2007
Externally publishedYes



  • Acylation
  • Catalytic triad
  • Hydrolysis
  • Lipase
  • Molecular orbital calculation
  • Tetrahedral intermediate

ASJC Scopus subject areas

  • Chemistry(all)

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