EC 1.11.1.7 - Peroxidase

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IntEnz Enzyme Nomenclature
EC 1.11.1.7

Names

Accepted name:
peroxidase
Other names:
Japanese radish peroxidase
extensin peroxidase
guaiacol peroxidase
heme peroxidase
horseradish peroxidase (HRP)
lactoperoxidase
oxyperoxidase
protoheme peroxidase
pyrocatechol peroxidase
scopoletin peroxidase
plant peroxidase
soybean peroxidase (SBP)
Coprinus cinereus peroxidase
Arthromyces ramosus peroxidase
Systematic name:
phenolic donor:hydrogen-peroxide oxidoreductase

Reaction

Cofactor

Comments:

Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00394
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004601
CAS Registry Number: 9003-99-0
UniProtKB/Swiss-Prot: (193) [show] [UniProt]

References

  1. Kenten, R.H. and Mann, P.J.G.
    Simple method for the preparation of horseradish peroxidase.
    Biochem. J. 57: 347-348 (1954). [PMID: 13172193]
  2. Morrison, M., Hamilton, H.B. and Stotz, E.
    The isolation and purification of lactoperoxidase by ion exchange chromatography.
    J. Biol. Chem. 228: 767-776 (1957). [PMID: 13475358]
  3. Paul, K.G.
    Peroxidases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 8, Academic Press, New York, 1963, 227-274
  4. Tagawa, K., Shin, M. and Okunuki, K.
    Peroxidases from wheat germ.
    Nature 183: 111 (1959). [PMID: 13622706]
  5. Theorell, H.
    Preparation and properties of crystalline horseradish peroxidase.
    Ark. Kemi Mineral. Geol. 16A: 11 (1943).
  6. Farhangrazi, Z. S., Copeland, B. R., Nakayama, T., Amachi, T., Yamazaki, I., Powers, L. S.
    Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase.
    Biochemistry 33: 5647-5652 (1994). [PMID: 8180190]
  7. Aitken, M. D., Heck, P. E.
    Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenols.
    Biotechnol. Prog. 14: 487-492 (1998). [PMID: 9622531]
  8. Dunford, H.B.
    Heme peroxidases, Wiley-VCH, New York, 1999, 33-218
  9. Torres, E and Ayala, M.
    Biocatalysis based on heme peroxidases, Springer, Berlin, 2010, 7-110

[EC 1.11.1.7 created 1961, modified 2011]