Molecular basis of perhydrolase activity in serine hydrolases

Peter Bernhardt; Karl Hult; Romas J. Kazlauskas

doi:10.1002/anie.200463006

Molecular basis of perhydrolase activity in serine hydrolases

Peter Bernhardt, Karl Hult, Romas J. Kazlauskas

Biotechnology Institute

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64 Scopus citations

Abstract

(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.

Original language	English (US)
Pages (from-to)	2742-2746
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	44
Issue number	18
DOIs	https://doi.org/10.1002/anie.200463006
State	Published - Apr 29 2005

Keywords

Enzyme catalysis
Hydrolases
Molecular modeling
Mutagenesis
Peroxides

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abstract = "(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.",

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AU - Kazlauskas, Romas J.

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AB - (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.

KW - Enzyme catalysis

KW - Hydrolases

KW - Molecular modeling

KW - Mutagenesis

KW - Peroxides

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Molecular basis of perhydrolase activity in serine hydrolases

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