Chloride peroxidase
| Chloride peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.11.1.10 | ||||||||
| CAS no. | 9055-20-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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:
- 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.[2][3]
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.[4]
The heme-containing chloroperoxidase (CPO) exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.[5] 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 PDB: 1A7U, PDB: 1A88, PDB: 1A8Q, PDB: 1A8S, PDB: 1A8U, PDB: 1BRT, PDB: 1CPO, PDB: 1IDQ, PDB: 1IDU, PDB: 1QHB, PDB: 1QI9, PDB: 1VNC, PDB: 1VNE, PDB: 1VNF, PDB: 1VNG, PDB: 1VNH, PDB: 1VNI, PDB: 1VNS, PDB: 2CIV, PDB: 2CIW, PDB: 2CIX, PDB: 2CIY, PDB: 2CIZ, PDB: 2CJ0, PDB: 2CJ1, PDB: 2CJ2, PDB: 2CPO, PDB: 2J18, PDB: 2J19, and PDB: 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.
- ↑ Latham, Jonathan; Brandenburger, Eileen; Shepherd, Sarah A.; Menon, Binuraj R. K.; Micklefield, Jason (2018). "Development of Halogenase Enzymes for Use in Synthesis". Chemical Reviews. 118 (1): 232–269. doi:10.1021/acs.chemrev.7b00032. PMID 28466644.
- ↑ Agarwal, Vinayak; Miles, Zachary D.; Winter, Jaclyn M.; Eustáquio, Alessandra S.; El Gamal, Abrahim A.; Moore, Bradley S. (2017). "Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse". Chemical Reviews. 117 (8): 5619–5674. doi:10.1021/acs.chemrev.6b00571. PMC 5575885. PMID 28106994.
- ↑ 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. doi:10.1016/S0021-9258(18)96701-3. 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.
