Estimation of the lipase PS (Pseudomonas cepacia) active site dimensions based on molecular mechanics calculations

X. Grabuleda, C. Jaime, A. Guerrero

Research output: Contribution to journalArticleResearchpeer-review

19 Citations (Scopus)

Abstract

Estimation of the active site dimensions of lipase PS (Amano) has been carried out for the first time through molecular modelling studies. The proposed model has been based on secondary alcohols, which are efficiently enantiodifferentiated by the enzyme as substrates. Some molecules which are not good substrates for the enzyme have also been used to define more precisely the limits of the active site. The model comprises three well- defined pockets: a large hydrophobic pocket of 7 x 6.6 x 4.4 Å 3 to interact with large hydrophobic substituents; a more hydrophilic pocket of ca 1.8 x 1.8 x 1.5 Å 3 to bind the hydroxyl group and a tunnel-shaped hydrophobic pocket (2 Å wide and 1.9 Å high) able to accomodate long side chains. The latter pocket is unique among the active site models described so far for other enzymes, which are essentially cubic in space. The model is of predictive value and accounts for the enantioselectivity shown by the enzyme in transesterification reactions of secondary alcohols.
Original languageEnglish
Pages (from-to)3675-3683
JournalTetrahedron Asymmetry
Volume8
Issue number21
DOIs
Publication statusPublished - 13 Nov 1997

Fingerprint Dive into the research topics of 'Estimation of the lipase PS (Pseudomonas cepacia) active site dimensions based on molecular mechanics calculations'. Together they form a unique fingerprint.

  • Cite this