Suppressed Native Hydrolytic Activity of a Lipase to Reveal Promiscuous Michael Addition Activity in Water
2009 (English)In: CHEMCATCHEM, ISSN 1867-3880, Vol. 1, no 2, 252-258 p.Article in journal (Refereed) Published
Suppression of,the,native hydrolytic activity of Pseudozyma antarctica lipase B (PalB) (formerly Candida antarctica lipase B) in water is demonstrated. By replacing the catalytic Ser 105 residue with an alanine unit, promiscuous Michael addition activity is favored. A Michael addition reaction between methyl acrylate and acetylacetone was explored as a model system. For the PalB Ser 105 Ala mutant, the hydrolytic activity was suppressed more than 1000 times and at the same time, the Michael addition activity was increased by a factor of 100. Docking studies and molecular dynamics simulations revealed an increased ability of the PalB Ser 105 Ala mutant to harbor the substrates close to a catalytically competent conformation.
Place, publisher, year, edition, pages
2009. Vol. 1, no 2, 252-258 p.
enzyme catalysis, enzyme promiscuity, lipases, Michael addition, molecular modeling, CANDIDA-ANTARCTICA, PYRIMIDINE-DERIVATIVES, CATALYTIC PROMISCUITY, ALKALINE PROTEASE, BACILLUS-SUBTILIS, ORGANIC MEDIA, OLD ENZYMES, FORCE-FIELD, BIOCATALYSIS
IdentifiersURN: urn:nbn:se:kth:diva-13269DOI: 10.1002/cctc.200900041ISI: 000274153900009ScopusID: 2-s2.0-77958074145OAI: oai:DiVA.org:kth-13269DiVA: diva2:323010