Molecular basis of perhydrolase activity in serine hydrolases

Peter Bernhardt, Karl Hult, Romas J. Kazlauskas

Research output: Contribution to journalArticlepeer-review

52 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 languageEnglish (US)
Pages (from-to)2742-2746
Number of pages5
JournalAngewandte Chemie - International Edition
Volume44
Issue number18
DOIs
StatePublished - Apr 29 2005

Keywords

  • Enzyme catalysis
  • Hydrolases
  • Molecular modeling
  • Mutagenesis
  • Peroxides

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