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Understanding the Plasticity of the alpha/beta Hydrolase Fold: Lid Swapping on the Candida antarctica Lipase B Results in Chimeras with Interesting Biocatalytic Properties
KTH, School of Biotechnology (BIO), Biochemistry.
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2009 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 10, no 3, 520-527 p.Article in journal (Refereed) Published
Abstract [en]

The Candida antarctica lipase B (CALB) has found very extensive use in biocatalysis reactions. Long molecular dynamics simulations of CALB in explicit aqueous solvent confirmed the high mobility of the regions lining the channel that leads into the active site, in particular, of helices alpha 5 and alpha 10. The simulation also confirmed the function of helix alpha 5 as a lid of the lipase. Replacing it with corresponding lid regions from the CALB homologues from Neurospora crassa and Gibberella zeae resulted in two new CALB mutants. Characterization of these revealed several interesting properties, including increased hydrolytic activity on simple esters, specifically substrates with C. branching on the carboxylic side, and much increased enantioselectivity in hydrolysis of racemic ethyl 2-phenylpropanoate (E > 50), which is a common structure of the profen drug family.

Place, publisher, year, edition, pages
2009. Vol. 10, no 3, 520-527 p.
Keyword [en]
enantioselectivity, enzyme catalysis, ester hydrolysis, gene expression, molecular dynamics
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-32685DOI: 10.1002/cbic.200800668ISI: 000263803100017Scopus ID: 2-s2.0-60349109395OAI: oai:DiVA.org:kth-32685DiVA: diva2:411432
Note
QC 20110418Available from: 2011-04-18 Created: 2011-04-18 Last updated: 2011-04-18Bibliographically approved

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