Molecular Basis of Perhydrolase Activity in Serine Hydrolases | Zendy

Bernhardt Peter | Zendy; Hult Karl | Zendy; Kazlauskas Romas J. | Zendy

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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.

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