2-haloacid dehalogenase (configuration-inverting)

From Wikipedia, the free encyclopedia
Jump to: navigation, search
2-haloacid dehalogenase (configuration-inverting)
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

2-haloacid dehalogenase (configuration-inverting) (EC, 2-haloalkanoic acid dehalogenase, 2-haloalkanoid acid halidohydrolase, DL-2-haloacid dehalogenase, DL-2-haloacid dehalogenase (inversion of configuration), DL-2-haloacid halidohydrolase (inversion of configuration), DL-DEXi, (R,S)-2-haloacid dehalogenase (configuration-inverting)) is an enzyme with systematic name (S)-2-haloacid dehalogenase (configuration-inverting).[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction

(1) (S)-2-haloacid + H2O (R)-2-hydroxyacid + halide
(2) (R)-2-haloacid + H2O (S)-2-hydroxyacid + halide

This enzyme dehalogenates both (S)- and (R)-2-haloalkanoic acids.


  1. ^ Motosugi, K.; Esahi, N.; Soda, K. (1982). "Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase". Arch. Microbiol. 131: 179–183. doi:10.1007/BF00405875. PMID 7103659. 
  2. ^ Motosugi, K.; Esahi, N.; Soda, K. (1982). "Purification and properties of a new enzyme, DL-2-haloacid dehalogenase, from Pseudomonas sp". J. Bacteriol. 150 (2): 522–527. PMC 216397Freely accessible. PMID 7068529. 
  3. ^ Motosugi, K.; Esahi, N.; Soda, K. (1984). "Enzymatic preparation of D- and L-lactic acid from racemic 2-chloropropionic acid". Biotechnol. Bioeng. 26 (7): 805–806. doi:10.1002/bit.260260729. 
  4. ^ 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. 
  5. ^ Liu, J.-Q.; Kurihara, T.; Hasan, A.K.M.Q.; Nardi-Dei, V.; Koshikawa, H.; Esaki, N.; Soda, K. (1994). "Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL". Appl. Environ. Microbiol. 60 (7): 2389–2393. PMC 201661Freely accessible. PMID 8074519. 
  6. ^ Cairns, S.S.; Cornish, A.; Cooper, R.A. (1996). "Cloning, sequencing and expression in Escherichia coli of two Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite stereospecificity". Eur. J. Biochem. 235 (3): 744–749. doi:10.1111/j.1432-1033.1996.t01-1-00744.x. PMID 8654424. 
  7. ^ Leigh, J.A.; Skinner, A.J.; Cooper, R.A. (1988). "Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species". FEMS Microbiol. Lett. 49: 353–356. doi:10.1111/j.1574-6968.1988.tb02756.x. 
  8. ^ Weightman, A.J.; Weightman, A.L.; Slater, J.H. (1982). "Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: evidence for two different dehalogenation mechanisms". J. Gen. Microbiol. 128 (8): 1755–1762. doi:10.1099/00221287-128-8-1755. PMID 7142958. 
  9. ^ Soda, K.; Kurihara, T.; 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: 2097–2103. doi:10.1351/pac199668112097. 

External links[edit]