(R)-2-haloacid dehalogenase
| (R)-2-haloacid dehalogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.8.1.9 | ||||||||
| CAS no. | 119345-29-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a (R)-2-haloacid dehalogenase (EC 3.8.1.9), DL-2-haloacid halidohydrolase (inversion of configuration), DL-DEXi, (R,S)-2-haloacid dehalogenase (configuration-inverting)) is an enzyme that catalyzes the chemical reaction
- (R)-2-haloacid + H2O (S)-2-hydroxyacid + halide
Thus, the two substrates of this enzyme are (R)-2-haloacid and H2O, whereas its two products are (S)-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 (R)-2-haloacid halidohydrolase. Other names in common use include 2-haloalkanoic acid dehalogenase[ambiguous], 2-haloalkanoid acid halidohydrolase[ambiguous], D-2-haloacid dehalogenase, and D-DEX.
D-DEXs lead to the production of 2-hydroxyacids and the release of halide ions from catalysing D-2-haloacid dehalogenation. D-DEXs are part of Group I dehalogenases, and this is due to similarity of the amino acid sequence. The D-DEX production of L-2-chloropropionic acid as an intermediate is related to herbicide production, there is a 30% similarity between DL-DEXs and D-DEXs in structure, and differences in DL-DEXs and D-DEXs are due to structural differences of the helical bend and the loop.[1]
References
- ↑ Wang, Yayue; Feng, Yanbin; Cao, Xupeng; Liu, Yinghui; Xue, Song (2018). "Insights into the molecular mechanism of dehalogenation catalyzed by D-2-haloacid dehalogenase from crystal structure". Scientific Reports.
- Smith JM, Harrison K, Colby J (1990). "Purification and characterization of D-2-haloacid dehalogenase from Pseudomonas putida strain AJ1/23". J. Gen. Microbiol. 136 (5): 881–6. doi:10.1099/00221287-136-5-881. PMID 2380688.
- Leigh JA, Skinner AJ, Cooper RA (1988). "Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species". FEMS Microbiol. Lett. 49 (3): 353–356. doi:10.1111/j.1574-6968.1988.tb02756.x.
- Soda, K.; Kurihara, Tatsuo; Liu, J.-Q.; Nardi-Dei, V.; Park, C.; Miyagi, 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.