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Molecular Basis of Perhydrolase Activity in Serine Hydrolases

Authors

  • Peter Bernhardt M.Sc.,

    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
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  • Karl Hult Prof. Dr.,

    1. School of Biotechnology, Department of Biochemistry, Royal Institute of Technology (KTH), AlbaNova University Center, Roslagstullsbacken 21, 10691 Stockholm, Sweden
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  • Romas J. Kazlauskas Prof. Dr.

    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
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  • We thank the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) and the University of Minnesota for financial support, the Minnesota Supercomputing Institute for computer modeling resources, C. Savile for advice and discussions, and M. Smith and J. Gosse for initial work.

Abstract

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Substratwechsel: Durch eine Mutation, die zu einer cis-Prolin-Peptidbindung in einer Schleifenstruktur nahe am aktiven Zentrum einer Arylesterase aus Pseudomonas fluorescens führt, wird aus dem Enzym eine Perhydrolase (siehe Bild). Das Umschalten der Aktivität wird mit einer neuen Wasserstoffbrücke zwischen einem Rückgrat-Carbonylsauerstoffatom und dem peroxidischen Desacylierungsintermediat erklärt.

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