Dehalogenase

From Proteopedia

spinqualitylabelsall models Structure of haloalkane dehalogenase complex with I- ion (purple) (PDB code 2edc). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights 5 3D structures of dehalogenase Function Dehalogenases catalyze the removal of halogen atom from substrates. • Haloalkane dehalogenase converts haloalkanes to alcohol[1] • Halohydrin dehalogenase converts halohydrins to epoxide[2] • L-2 haloacid dehalogenase converts L-2-haloacids to D-2-hydroxyacid[3] • S-2 haloacid dehalogenase converts S-2-haloacids to R-2-hydroxyacid • 4-chlorobenzoyl CoA dehalogenase converts 4-chlorobenzoyl CoA to 4-hydroxybenzoyl CoA [4] • Fluoroacetate dehalogenase converts fluoroacetate to glycolate[5] • Iodotyrosine dehalogenase converts iodotyrosine to tyrosine[6] • cis- and trans-3-chloroacrylic acid dehalogenase converts 3-chloroacrylate to malonate semialdehyde • 5-chloromuconolactone dehalogenase converts 5-chloromuconolactone to E-dienelactone[7] • Tetrachloroethene reductive dehalogenase catalyzes the conversion of trichloroethene, Cl- and acceptor to tetrachloroethene and reduced acceptor[8]. Relevance Haloalkane dehalogenase is tested for the biodegredation of toxic industrial by-products. Fluoroacetate dehalogenase is tested for the biodegredation of the poisonous fluroacetate which can kill livestock and is found in some plants in Australia, Africa and Central America. Halohydrin dehalogenase is used as a biocatalyst. Disease Iodotyrosine dehalogenase mutation is involved in congenital hypothyroidism[9]. Structural highlights In the fluoroacetate dehalogenase complex with halide, the (in cyan).[10] 3D structures of dehalogenase Dehalogenase 3D structures

References

1. ↑ Koudelakova T, Chovancova E, Brezovsky J, Monincova M, Fortova A, Jarkovsky J, Damborsky J. Substrate specificity of haloalkane dehalogenases. Biochem J. 2011 Apr 15;435(2):345-54. doi: 10.1042/BJ20101405. PMID:21294712 doi:http://dx.doi.org/10.1042/BJ20101405
2. ↑ Schallmey A, Schallmey M. Recent advances on halohydrin dehalogenases-from enzyme identification to novel biocatalytic applications. Appl Microbiol Biotechnol. 2016 Sep;100(18):7827-39. doi:, 10.1007/s00253-016-7750-y. Epub 2016 Aug 8. PMID:27502414 doi:http://dx.doi.org/10.1007/s00253-016-7750-y
3. ↑ Liu JQ, Kurihara T, Miyagi M, Esaki N, Soda K. Reaction mechanism of L-2-haloacid dehalogenase of Pseudomonas sp. YL. Identification of Asp10 as the active site nucleophile by 18O incorporation experiments. J Biol Chem. 1995 Aug 4;270(31):18309-12. PMID:7629151
4. ↑ Lau EY, Bruice TC. The active site dynamics of 4-chlorobenzoyl-CoA dehalogenase. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9527-32. doi:, 10.1073/pnas.161282698. Epub 2001 Aug 7. PMID:11493680 doi:http://dx.doi.org/10.1073/pnas.161282698
5. ↑ Liu JQ, Kurihara T, Ichiyama S, Miyagi M, Tsunasawa S, Kawasaki H, Soda K, Esaki N. Reaction mechanism of fluoroacetate dehalogenase from Moraxella sp. B. J Biol Chem. 1998 Nov 20;273(47):30897-902. PMID:9812982
6. ↑ Gnidehou S, Caillou B, Talbot M, Ohayon R, Kaniewski J, Noel-Hudson MS, Morand S, Agnangji D, Sezan A, Courtin F, Virion A, Dupuy C. Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site. FASEB J. 2004 Oct;18(13):1574-6. Epub 2004 Aug 2. PMID:15289438 doi:http://dx.doi.org/10.1096/fj.04-2023fje
7. ↑ Ferraroni M, Kolomytseva M, Golovleva LA, Scozzafava A. X-ray crystallographic and molecular docking studies on a unique chloromuconolactone dehalogenase from Rhodococcus opacus 1CP. J Struct Biol. 2013 Apr;182(1):44-50. doi: 10.1016/j.jsb.2013.01.006. Epub 2013, Jan 30. PMID:23376735 doi:http://dx.doi.org/10.1016/j.jsb.2013.01.006
8. ↑ Miller E, Wohlfarth G, Diekert G. Purification and characterization of the tetrachloroethene reductive dehalogenase of strain PCE-S. Arch Microbiol. 1998 Jun;169(6):497-502. PMID:9575235
9. ↑ Afink G, Kulik W, Overmars H, de Randamie J, Veenboer T, van Cruchten A, Craen M, Ris-Stalpers C. Molecular characterization of iodotyrosine dehalogenase deficiency in patients with hypothyroidism. J Clin Endocrinol Metab. 2008 Dec;93(12):4894-901. doi: 10.1210/jc.2008-0865., Epub 2008 Sep 2. PMID:18765512 doi:http://dx.doi.org/10.1210/jc.2008-0865
10. ↑ Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW. Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry. 1993 Sep 7;32(35):9031-7. PMID:8369276