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Molecular basis of perhydrolase activity in serine hydrolases
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.
2005 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 44, no 18, 2742-2746 p.Article in journal (Refereed) Published
Abstract [en]

(Chemical Equation Presented) Changing substrates: A mutation that forms a cis-proline-peptide bond in a loop structure close to the active site of an aryl esterase from Pseudomonas fluorescens converts the enzyme into a perhydrolase (see picture). The switch in activity is explained by a new hydrogen bond formed between a backbone carbonyl oxygen atom and the peroxy deacylation intermediate.

Place, publisher, year, edition, pages
2005. Vol. 44, no 18, 2742-2746 p.
Keyword [en]
enzyme catalysis, hydrolases, molecular modeling, mutagenesis, peroxides
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-37743DOI: 10.1002/anie.200463006ISI: 000228957600017PubMedID: 15803517OAI: oai:DiVA.org:kth-37743DiVA: diva2:435061
Available from: 2011-08-17 Created: 2011-08-17 Last updated: 2017-12-08Bibliographically approved

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