| 词条 | Chloride peroxidase |
| 释义 |
| Name = Chloride peroxidase | EC_number = 1.11.1.10 | CAS_number = 9055-20-3 | IUBMB_EC_number = 1/11/1/10 | GO_code = | image = | width = | caption = }} Chloride peroxidase ({{EC number|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 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.[1] The heme-containing chloroperoxidase (CPO) exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.[2] 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 studiesAs of late 2007, 30 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1A7U}}, {{PDB link|1A88}}, {{PDB link|1A8Q}}, {{PDB link|1A8S}}, {{PDB link|1A8U}}, {{PDB link|1BRT}}, {{PDB link|1CPO}}, {{PDB link|1IDQ}}, {{PDB link|1IDU}}, {{PDB link|1QHB}}, {{PDB link|1QI9}}, {{PDB link|1VNC}}, {{PDB link|1VNE}}, {{PDB link|1VNF}}, {{PDB link|1VNG}}, {{PDB link|1VNH}}, {{PDB link|1VNI}}, {{PDB link|1VNS}}, {{PDB link|2CIV}}, {{PDB link|2CIW}}, {{PDB link|2CIX}}, {{PDB link|2CIY}}, {{PDB link|2CIZ}}, {{PDB link|2CJ0}}, {{PDB link|2CJ1}}, {{PDB link|2CJ2}}, {{PDB link|2CPO}}, {{PDB link|2J18}}, {{PDB link|2J19}}, and {{PDB link|2J5M}}. References1. ^{{Cite journal|journal = Natural Product Reports|year = 2004|volume = 21|issue = 1|pmid = 15039842|doi = 10.1039/b302337k|title = The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products|first = Alison|last = Butler|author2=Carter-Franklin, Jayme N.|pages = 180–8}} (this paper also discussed chloroperoxidases. 2. ^{{cite journal |doi=10.1016/S0969-2126(01)00274-X |vauthors=Poulos TL, Sundaramoorthy M, Terner J |title=The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid |journal=Structure |volume=3 |issue=12 |pages=1367–1377 |year=1995 |pmid=8747463}} Further reading
3 : EC 1.11.1|Heme enzymes|Enzymes of known structure |
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