Haloacetate dehalogenase
| haloacetate dehalogenase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.8.1.3 | ||||||||
| CAS number | 37289-40-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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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.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1Y37.
References
- 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 (23): 5557–9. PMID 5928195.
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