Molecular basis of perhydrolase activity in serine hydrolases

Peter Bernhardt, Karl Hult, Romas J. Kazlauskas

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


(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
Issue number18
StatePublished - Apr 29 2005


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


Dive into the research topics of 'Molecular basis of perhydrolase activity in serine hydrolases'. Together they form a unique fingerprint.

Cite this