Crystal structure of the haloalkane dehalogenase DbjA
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چکیده
منابع مشابه
Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: the effect of pH and temperature.
The effect of pH and temperature on structure, stability, activity and enantioselectivity of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110 was investigated in this study. Conformational changes have been assessed by circular dichroism spectroscopy, functional changes by kinetic analysis, while quaternary structure was studied by gel filtration chromatography. Our study show...
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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...
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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...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305091786