Haloacetate dehalogenase
From Wikipedia, the free encyclopedia
In enzymology, a haloacetate dehalogenase (EC 3.8.1.3) is an enzyme that catalyzes the chemical reaction
- haloacetate + H2O glycolate + halide
Thus, the two substrates of this enzyme are haloacetate and H2O, whereas its two products are glycolate and halide.
This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is haloacetate halidohydrolase. This enzyme is also called monohaloacetate dehalogenase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,2-dichloroethane degradation.
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[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1Y37.
[edit] References
- IUBMB entry for 3.8.1.3
- BRENDA references for 3.8.1.3 (Recommended.)
- PubMed references for 3.8.1.3
- PubMed Central references for 3.8.1.3
- Google Scholar references for 3.8.1.3
- GOLDMAN P (1965). "THE ENZYMATIC CLEAVAGE OF THE CARBON-FLUORINE BOND IN FLUOROACETATE". J. Biol. Chem. 240: 3434–8. PMID 14321384.
- Goldman P, Milne GW (1966). "Carbon-fluorine bond cleavage. II. Studies on the mechanism of the defluorination of fluoroacetate". J. Biol. Chem. 241: 5557–9. PMID 5928195.
[edit] External links
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- The CAS registry number for this enzyme class is 37289-40-0.