Switched enantiopreference of Humicola lipase for 2-phenoxyalkanoic acid ester homologs can be rationalized by different substrate binding modes
1999 (English)In: Tetrahedron: asymmetry, ISSN 0957-4166, E-ISSN 1362-511X, Vol. 10, no 21, 4191-4202 p.Article in journal (Refereed) Published
Humicola lanuginosa lipase was used for enantioselective hydrolyses of a series of homologous 2-phenoxyalkanoic acid ethyl esters. The enantioselectivity (E-value) of the enzyme changed from an (R)-enantiomer preference for the smallest substrate, 2-phenoxypropanoic acid ester, to an (S)-enantiomer preference for the homologous esters with longer acyl moieties. The E-values span the range from E=13 (R) to E=56 (S). A molecular modeling study identified two different substrate-binding modes for each enantiomer. We found that the enantiomers favored different modes. This discovery provided a model that offered a rational explanation for the observed switch in enantioselectivity. (C) 1999 Elsevier Science Ltd. All rights reserved.
Place, publisher, year, edition, pages
1999. Vol. 10, no 21, 4191-4202 p.
CANDIDA-RUGOSA LIPASE, LANUGINOSA LIPASE, QUANTITATIVE-ANALYSES, SUBTILISIN CARLSBERG, NUCLEIC-ACIDS, FORCE-FIELD, ENANTIOMERS, BIOCATALYSIS, RESOLUTION, BIOTRANSFORMATIONS
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-25181ISI: 000083948700019OAI: oai:DiVA.org:kth-25181DiVA: diva2:356311
QC 20101012 NR 201408042010-10-122010-10-122012-02-03Bibliographically approved