Premium
Molecular Basis of Perhydrolase Activity in Serine Hydrolases
Author(s) -
Bernhardt Peter,
Hult Karl,
Kazlauskas Romas J.
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200463006
Subject(s) - pseudomonas fluorescens , serine , chemistry , stereochemistry , active site , esterase , proline , hydrogen bond , enzyme , mutation , oxygen atom , biochemistry , molecule , biology , organic chemistry , amino acid , bacteria , genetics , gene
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.