Molecular Basis of Perhydrolase Activity in Serine Hydrolases

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 backb...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2005-04, Vol.44 (18), p.2742-2746
Main Authors: Bernhardt, Peter, Hult, Karl, Kazlauskas, Romas J.
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biokemi
Chemistry
enzyme catalysis
Esterases - chemistry
Esters - metabolism
hydrolases
Hydrolases - chemistry
Hydrolases - metabolism
Hydrolysis
Kemi
Kinetics
Models, Molecular
molecular modeling
Molecular Structure
mutagenesis
NATURAL SCIENCES
NATURVETENSKAP
Peracetic Acid - chemistry
Peracetic Acid - metabolism
peroxides
Protein Structure, Tertiary
Pseudomonas fluorescens - enzymology
Rats
Serine - metabolism
Structure-Activity Relationship
Substrate Specificity
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Summary: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.
ISSN:1433-7851
1521-3773
1521-3773
DOI:10.1002/anie.200463006