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.
Original language | English |
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Pages (from-to) | 163-191 |
Number of pages | 29 |
Journal | Annual Review of Microbiology |
Volume | 48 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1994 |
Keywords
- DEHALOGENASE
- CHLORINATED HYDROCARBONS
- ADAPTATION
- BIODEGRADATION
- DECHLORINATION
- HALOGENATED COMPOUNDS
- XANTHOBACTER-AUTOTROPHICUS GJ10
- PSEUDOMONAS-PUTIDA PP3
- 2-HALOALKANOIC ACID DEHALOGENASE
- 2-HALOACID HALIDOHYDROLASE IVA
- SP STRAIN CBS3
- HALOALKANE DEHALOGENASE
- SEQUENCE-ANALYSIS
- DICHLOROMETHANE DEHALOGENASE
- GAMMA-HEXACHLOROCYCLOHEXANE
- MICROBIAL-DEGRADATION