Crystal structure of the haloalkane dehalogenase fromSphingomonas paucimobilisUT26
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چکیده
منابع مشابه
Structure and activity of DmmA, a marine haloalkane dehalogenase.
DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected with 1,3-dibromopropane as substrate, with steady-state kinetic parameters typical of HLDs (K(m) = 0.24 ± 0.05 mM, k(cat) = 2.4 ± 0.1 s(-1) ). The 2.2-Å crystal structure of DmmA revealed a fold and active site similar to other HLDs...
متن کاملCrystal structure and site - directed mutagenesis analyses of haloalkane 1 dehalogenase LinB from Sphingobium sp .
To whom correspondence should be addressed: Masaru Tanokura, Department of Applied 11 Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of 12 Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan Tel: 81-3-5841-5165; Fax: 13 81-3-5841-8023; E-mail: [email protected] 14 Copyright © 2013, American Society for Microbiology. All Rights Reserved. J. Bact...
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Haloalkane dehalogenases (HLDs) have recently been discovered in a number of bacteria, including symbionts and pathogens of both plants and humans. However, the biological roles of HLDs in these organisms are unclear. The development of efficient HLD inhibitors serving as molecular probes to explore their function would represent an important step toward a better understanding of these interest...
متن کاملSpecificity and kinetics of haloalkane dehalogenase.
Haloalkane dehalogenase converts halogenated alkanes to their corresponding alcohols. The active site is buried inside the protein and lined with hydrophobic residues. The reaction proceeds via a covalent substrate-enzyme complex. This paper describes a steady-state and pre-steady-state kinetic analysis of the conversion of a number of substrates of the dehalogenase. The kinetic mechanism for t...
متن کاملRepositioning the catalytic triad aspartic acid of haloalkane dehalogenase: effects on stability, kinetics, and structure.
Haloalkane dehalogenase (DhlA) catalyzes the hydrolysis of haloalkanes via an alkyl-enzyme intermediate. The covalent intermediate, which is formed by nucleophilic substitution with Asp124, is hydrolyzed by a water molecule that is activated by His289. The role of Asp260, which is the third member of the catalytic triad, was studied by site-directed mutagenesis. Mutation of Asp260 to asparagine...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2000
ISSN: 0108-7673
DOI: 10.1107/s0108767300025332