Molecular basis of perhydrolase activity in serine hydrolases

Angew Chem Int Ed Engl. 2005 Apr 29;44(18):2742-2746. doi: 10.1002/anie.200463006.

Authors

Peter Bernhardt^{1

2}, Karl Hult², Romas J Kazlauskas¹

Affiliations

¹ University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, The Biotechnology Institute, and The Center for Microbial and Plant Genomics, 1479 Gortner Avenue, St. Paul, Minnesota 55108, USA, Fax: (+1) 612-625-5780.
² School of Biotechnology, Department of Biochemistry, Royal Institute of Technology (KTH), AlbaNova University Center, Roslagstullsbacken 21, 10691 Stockholm, Sweden.

PMID: 15803517
DOI: 10.1002/anie.200463006

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Esterases / chemistry
Esters / metabolism
Hydrolases / chemistry
Hydrolases / metabolism*
Hydrolysis
Kinetics
Models, Molecular
Molecular Structure
Peracetic Acid / chemistry
Peracetic Acid / metabolism
Protein Structure, Tertiary
Pseudomonas fluorescens / enzymology
Rats
Serine / metabolism*
Structure-Activity Relationship
Substrate Specificity

Substances

Esters
Serine
Hydrolases
Esterases
Peracetic Acid