(S)-2-haloacid dehalogenase
| (S)-2-haloacid dehalogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.8.1.2 | ||||||||
| CAS number | 37289-39-7 | ||||||||
| 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 (S)-2-haloacid dehalogenase (EC 3.8.1.2) is an enzyme that catalyzes the chemical reaction
- (S)-2-haloacid + H2O (R)-2-hydroxyacid + halide
Thus, the two substrates of this enzyme are (S)-2-haloacid and H2O, whereas its two products are (R)-2-hydroxyacid 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 (S)-2-haloacid halidohydrolase. Other names in common use include 2-haloacid dehalogenase[ambiguous], 2-haloacid halidohydrolase [ambiguous][ambiguous], 2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, 2-halocarboxylic acid dehalogenase II, DL-2-haloacid dehalogenase[ambiguous], L-2-haloacid dehalogenase, and L-DEX. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,2-dichloroethane degradation.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1AQ6, 1JUD, 1QH9, 1QQ5, 1QQ6, 1QQ7, 1ZRM, 1ZRN, 2NO4, and 2NO5.
References
- Goldman P, Milne GW, Keister DB (1968). "Carbon-halogen bond cleavage. 3. Studies on bacterial halidohrolases". J. Biol. Chem. 243 (2): 428–34. PMID 5635785.
- Motosugi M, Esaki N, Soda K (1982). "Preparation and properties of 2-halo acid dehalogenase from Pseudomonas putida". Agric. Biol. Chem. 46: 837–838. doi:10.1271/bbb1961.46.837.
- Klages U, Krauss S, Lingens F (1983). "2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3". Hoppe. Seylers. Z. Physiol. Chem. 364 (5): 529–35. doi:10.1515/bchm2.1983.364.1.529. PMID 6873881.
- Diez A, Prieto MI, Alvarez MJ, Bautista JM, Garrido J, Puyet A (1996). "Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation". Biochem. Biophys. Res. Commun. 220 (3): 828–33. doi:10.1006/bbrc.1996.0489. PMID 8607850.
- Morsberger FM, Muller R, Otto MK, Lingens F, Kulbe KD (1991). "Purification and characterization of 2-halocarboxylic acid dehalogenase II from Pseudomonas spec. CBS 3". Biol. Chem. Hoppe-Seyler. 372 (10): 915–22. doi:10.1515/bchm3.1991.372.2.915. PMID 1772590.
- Kohler R, Brokamp A, Schwarze R, Reiting RH, Schmidt FR (1998). "Characteristics and DNA-sequence of a cryptic haloalkanoic acid dehalogenase from Agrobacterium tumefaciens RS5". Curr. Microbiol. 36 (2): 96–101. doi:10.1007/s002849900286. PMID 9425247.
- Motosugi K, Esaki N, Soda K (1982). "Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase". Arch. Microbiol. 131 (3): 179–83. doi:10.1007/BF00405875. PMID 7103659.
- Kurihara T, Esaki N, Soda K (2000). "Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms". J. Mol. Catal., B Enzym. 10: 57–65. doi:10.1016/S1381-1177(00)00108-9.
- M, Tsunasawa S; Esaki N (1996). "Bacterial 2-haloacid dehalogenases: Structures and catalytic properties". Pure Appl. Chem. 68 (11): 2097–2103. doi:10.1351/pac199668112097.