(S)-2-haloacid dehalogenase
| (S)-2-haloacid dehalogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.8.1.2 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
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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
[edit]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
[edit]- Goldman P, Milne GW, Keister DB (1968). "Carbon-halogen bond cleavage. 3. Studies on bacterial halidohrolases". J. Biol. Chem. 243 (2): 428–34. doi:10.1016/S0021-9258(18)99310-5. PMID 5635785.
- Motosugi M, Esaki N, Soda K (1982). "Preparation and properties of 2-halo acid dehalogenase from Pseudomonas putida". Agric. Biol. Chem. 46 (3): 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-Seyler's 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. S2CID 12691244.
- 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. Bibcode:1982ArMic.131..179M. doi:10.1007/BF00405875. PMID 7103659. S2CID 35346002.
- Kurihara T, Esaki N, Soda K (2000). "Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms". J. Mol. Catal., B Enzym. 10 (1–3): 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. S2CID 38522855.
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