Literature DB >> 7826004

Genetics and biochemistry of dehalogenating enzymes.

D B Janssen1, F Pries, J R van der Ploeg.   

Abstract

Microorganisms that can utilize halogenated compounds as a growth substrate generally produce-enzymes whose function is carbon-halogen bond cleavage. Based on substrate range, reaction type and gene sequences, the dehalogenating enzymes can be classified in different groups, including hydrolytic dehalogenases, glutathione transferases, monooxygenases and hydratases. X-ray crystallographic and biochemical studies have provided detailed mechanistic insight into the action of haloalkane dehalogenase. The essential features are nucleophilic substitution of the halogen by a carboxylate group and the presence of a distinct halogen binding site, formed by tryptophan residues. This review summaries current knowledge on a variety of other dehalogenating enzymes and indicates the existence of a widespread and diverse microbial potential for dechlorination of natural and xenobiotic halogenated compounds.

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Year:  1994        PMID: 7826004     DOI: 10.1146/annurev.mi.48.100194.001115

Source DB:  PubMed          Journal:  Annu Rev Microbiol        ISSN: 0066-4227            Impact factor:   15.500


  25 in total

1.  Reconstruction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB.

Authors:  Yuji Nagata; Zbynek Prokop; Sona Marvanová; Jana Sýkorová; Marta Monincová; Masataka Tsuda; Jirí Damborský
Journal:  Appl Environ Microbiol       Date:  2003-04       Impact factor: 4.792

2.  Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: gene cloning and structural comparison with D- and L-2-haloacid dehalogenases.

Authors:  V Nardi-Dei; T Kurihara; C Park; N Esaki; K Soda
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

3.  Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities.

Authors:  Yukari Sato; Marta Monincová; Radka Chaloupková; Zbynek Prokop; Yoshiyuki Ohtsubo; Kiwamu Minamisawa; Masataka Tsuda; Jirí Damborsky; Yuji Nagata
Journal:  Appl Environ Microbiol       Date:  2005-08       Impact factor: 4.792

4.  Dehalogenation of haloalkanes by Mycobacterium tuberculosis H37Rv and other mycobacteria.

Authors:  A Jesenská; I Sedlácek; J Damborský
Journal:  Appl Environ Microbiol       Date:  2000-01       Impact factor: 4.792

5.  NADPH-dependent reductive ortho dehalogenation of 2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and Coryneform bacterium strainNTB-1 via 2,4-dichlorobenzoyl coenzyme A.

Authors:  V Romanov; R P Hausinger
Journal:  J Bacteriol       Date:  1996-05       Impact factor: 3.490

6.  Sequence analysis of the upstream region of dhlB, the gene encoding haloalkanoic acid dehalogenase of Xanthobacter autotrophicus GJ10.

Authors:  J van der Ploeg; D B Janssen
Journal:  Biodegradation       Date:  1995-09       Impact factor: 3.909

7.  Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene families.

Authors:  K E Hill; J R Marchesi; A J Weightman
Journal:  J Bacteriol       Date:  1999-04       Impact factor: 3.490

8.  Reductive, coenzyme A-mediated pathway for 3-chlorobenzoate degradation in the phototrophic bacterium Rhodopseudomonas palustris.

Authors:  P G Egland; J Gibson; C S Harwood
Journal:  Appl Environ Microbiol       Date:  2001-03       Impact factor: 4.792

9.  The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability.

Authors: 
Journal:  Proc Natl Acad Sci U S A       Date:  2003-09-18       Impact factor: 11.205

10.  Dechlorination of chloral hydrate is influenced by the biofilm adhesin protein LapA in Pseudomonas putida LF54.

Authors:  Wanjun Zhang; Yuanbai Pan; Masanori Toyofuku; Nobuhiko Nomura; Toshiaki Nakajima; Hiroo Uchiyama
Journal:  Appl Environ Microbiol       Date:  2013-04-19       Impact factor: 4.792

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