EC 1.11.1.10 - Chloride peroxidase

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IntEnz Enzyme Nomenclature
EC 1.11.1.10

Names

Accepted name:
chloride peroxidase
Other names:
chloroperoxidase
CPO
vanadium haloperoxidase
Systematic name:
chloride:hydrogen-peroxide oxidoreductase

Reaction

Cofactor

Comments:

Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC51405
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016691
CAS Registry Number: 9055-20-3
UniProtKB/Swiss-Prot:

References

  1. Hager, L.P., Hollenberg, P.F., Rand-Meir, T., Chiang, R. and Doubek, D.L.
    Chemistry of peroxidase intermediates.
    Ann. N.Y. Acad. Sci. 244: 80-93 (1975). [PMID: 1056179]
  2. Morris, D.R. and Hager, L.P.
    Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein.
    J. Biol. Chem. 241: 1763-1768 (1966). [PMID: 5949836]
  3. Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F.
    Halohydrocarbon synthesis by homoperoxidase.
    Science 202: 1094-1096 (1978). [PMID: 17777960]
  4. Sundaramoorthy, M., Terner, J., Poulos, T. L.
    The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
    Structure 3: 1367-1377 (1995). [PMID: 8747463]
  5. ten Brink, H. B., Tuynman, A., Dekker, H. L., Hemrika, W., Izumi, Y., Oshiro, T., Schoemaker, H. E., Wever, R.
    Enantioselective sulfoxidation catalyzed by vanadium haloperoxidases.
    Inorg Chem 37: 6780-6784 (1998). [PMID: 11670813]
  6. ten Brink, H. B., Dekker, H. L., Schoemaker, H. E., Wever, R.
    Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis.
    J. Inorg. Biochem. 80: 91-98 (2000). [PMID: 10885468]
  7. Murali Manoj, K.
    Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process.
    Biochim. Biophys. Acta 1764: 1325-1339 (2006). [PMID: 16870515]
  8. Kühnel, K., Blankenfeldt, W., Terner, J., Schlichting, I.
    Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.
    J. Biol. Chem. 281: 23990-23998 (2006). [PMID: 16790441]
  9. Manoj, K. M., Hager, L. P.
    Chloroperoxidase, a janus enzyme.
    Biochemistry 47: 2997-3003 (2008). [PMID: 18220360]

[EC 1.11.1.10 created 1972, modified 2011]