Summary
Chloride peroxidase (EC 1.11.1.10) is a family of enzymes that catalyzes the chlorination of organic compounds. This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate:
| Chloride peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.11.1.10 | ||||||||
| CAS no. | 9055-20-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O
In fact the source of "Cl+" is hypochlorous acid (HOCl).[1] Many organochlorine compounds are biosynthesized in this way.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptors (peroxidases). The systematic name of this enzyme class is chloride:hydrogen-peroxide oxidoreductase. This enzyme is also called chloroperoxidase. It employs one cofactor which may be either heme or vanadium.[2]
The heme-containing chloroperoxidase (CPO) exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.[3] Despite functional similarities with other heme enzymes, the structure of CPO is unique, which folds into a tertiary structure dominated by eight helical segments. The catalytic acid base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in horseradish peroxidase.
Structural studies edit
As of late 2007, 30 structures have been solved for this class of enzymes, with PDB accession codes 1A7U, 1A88, 1A8Q, 1A8S, 1A8U, 1BRT, 1CPO, 1IDQ, 1IDU, 1QHB, 1QI9, 1VNC, 1VNE, 1VNF, 1VNG, 1VNH, 1VNI, 1VNS, 2CIV, 2CIW, 2CIX, 2CIY, 2CIZ, 2CJ0, 2CJ1, 2CJ2, 2CPO, 2J18, 2J19, and 2J5M.
References edit
- ^ Hofrichter, M.; Ullrich, R.; Pecyna, Marek J.; Liers, Christiane; Lundell, Taina (2010). "New and classic families of secreted fungal heme peroxidases". Appl Microbiol Biotechnol. 87 (3): 871–897. doi:10.1007/s00253-010-2633-0. PMID 20495915. S2CID 24417282.
- ^ Butler, Alison; Carter-Franklin, Jayme N. (2004). "The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products". Natural Product Reports. 21 (1): 180–8. doi:10.1039/b302337k. PMID 15039842. (this paper also discussed chloroperoxidases.
- ^ Poulos TL, Sundaramoorthy M, Terner J (1995). "The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid". Structure. 3 (12): 1367–1377. doi:10.1016/S0969-2126(01)00274-X. PMID 8747463.
Further reading edit
- Hager LP, Hollenberg PF, Rand-Meir T, Chiang R, Doubek D (1975). "Chemistry of peroxidase intermediates". Ann. N. Y. Acad. Sci. 244 (1): 80–93. Bibcode:1975NYASA.244...80H. doi:10.1111/j.1749-6632.1975.tb41524.x. PMID 1056179. S2CID 27336177.
- Morris DR, Hager LP (1966). "Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein". J. Biol. Chem. 241 (8): 1763–8. PMID 5949836.
- Theiler R, Cook JC, Hager LP, Siuda JF (1978). "Halohydrocarbon synthesis by homoperoxidase". Science. 202 (4372): 1094–1096. Bibcode:1978Sci...202.1094T. doi:10.1126/science.202.4372.1094. PMID 17777960. S2CID 21448823.
