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Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications
Open accessAbstract
This review is a survey of bacterial dehalogenases that catalyze the cleavage of halogen substituents from haloaromatics, haloalkanes, haloalcohols, and haloalkanoic acids. Concerning the enzymatic cleavage of the carbon-halogen bond, seven mechanisms of dehalogenation are known, namely, reductive, oxygenolytic, hydrolytic, and thiolytic dehalogenation; intramolecular nucleophilic displacement; dehydrohalogenation; and hydration. Spontaneous dehalogenation reactions may occur as a result of chemical decomposition of unstable primary products of an unassociated enzyme reaction, and fortuitous dehalogenation can result from the action of broad-specificity enzymes converting halogenated analogs of their natural substrate. Reductive dehalogenation either is catalyzed by a specific dehalogenase or may be mediated by free or enzyme-bound transition metal cofactors (porphyrins, corrins). Desulfomonile tiedjei DCB-1 couples energy conservation to a reductive dechlorination reaction. The biochemistry and genetics of oxygenolytic and hydrolytic haloaromatic dehalogenases are discussed. Concerning the haloalkanes, oxygenases, glutathione S-transferases, halidohydrolases, and dehydrohalogenases are involved in the dehalogenation of different haloalkane compounds. The epoxide-forming halohydrin hydrogen halide lyases form a distinct class of dehalogenases. The dehalogenation of alpha-halosubstituted alkanoic acids is catalyzed by halidohydrolases, which, according to their substrate and inhibitor specificity and mode of product formation, are placed into distinct mechanistic groups. beta-Halosubstituted alkanoic acids are dehalogenated by halidohydrolases acting on the coenzyme A ester of the beta-haloalkanoic acid. Microbial systems offer a versatile potential for biotechnological applications. Because of their enantiomer selectivity, some dehalogenases are used as industrial biocatalysts for the synthesis of chiral compounds. The application of dehalogenases or bacterial strains in environmental protection technologies is discussed in detail.
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Citations
Cited by
BIODEGRADATION OF NITROAROMATIC COMPOUNDS
Spain, J. C. (1995) · Annual Review of Microbiology · doi:10.1146/annurev.mi.49.100195.002515 · Cited by 939
Reductive dechlorination in the energy metabolism of anaerobic bacteria
Holliger, C., Wohlfarth, G., & Diekert, G. (1998) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(98)00030-8 · Cited by 358
Developing a metagenomic view of xenobiotic metabolism
Haiser, H. J., & Turnbaugh, P. J. (2013) · Pharmacological Research · doi:10.1016/j.phrs.2012.07.009 · Cited by 186
“One well-studied enzyme class is a group called the dehalogenases that catalyze the cleavage of the halogen-carbon bond through a number of different mechanisms [20].”
BackgroundPurification and Characterization of Tetrachloroethene Reductive Dehalogenase from
Neumann, A., Wohlfarth, G., & Diekert, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16515 · Cited by 182
Gnidehou, S., Caillou, B., Talbot, M., Ohayon, R., Kaniewski, J., Noël‐Hudson, M., Morand, S., Agnangji, D., Sezan, A., Courtin, F., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-2023fje · Cited by 135
Metadata
- Authors
- Fetzner, S., & Lingens, F.
- Venue
- Microbiological Reviews
- Publisher
- American Society for Microbiology
- Published
- 1994-01-01
- Volume
- 58
- Issue
- 4
- Pages
- 641-685
- ISSN
- 0146-0749 (ISSN-L)
- OpenAlex
- W1961857851
- Cited by
- 459
- References
- 0
- FWCI
- 26.04
- Type
- journal article
- Language
- en
- Open access
- diamond
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- Fetzner, S., & Lingens, F. (1994). Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications. Microbiological Reviews. https://doi.org/10.1128/mmbr.58.4.641-685.1994
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