EC 1.11.1.6 - Catalase

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IntEnz Enzyme Nomenclature
EC 1.11.1.6

Names

Accepted name:
catalase
Other names:
CAT
caperase
catalase-peroxidase
equilase
optidase
Systematic name:
hydrogen-peroxide:hydrogen-peroxide oxidoreductase

Reaction

Cofactors

Comments:

A hemoprotein. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00395
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004096
CAS Registry Number: 9001-05-2
UniProtKB/Swiss-Prot: (146) [show] [UniProt]

References

  1. Herbert, D. and Pinsent, J.
    Crystalline bacterial catalase.
    Biochem. J. 43: 193-202 (1948). [PMID: 16748386]
  2. Herbert, D. and Pinsent, J.
    Crystalline human erythrocyte catalase.
    Biochem. J. 43: 203-205 (1948). [PMID: 16748387]
  3. Keilin, D. and Hartree, E.F.
    Coupled oxidation of alcohol.
    Proc. R. Soc. Lond. B Biol. Sci. 119: 141-159 (1936).
  4. Kono, Y. and Fridovich, I.
    Isolation and characterization of the pseudocatalase of Lactobacillus plantarum.
    J. Biol. Chem. 258: 6015-6019 (1983). [PMID: 6853475]
  5. Nicholls, P. and Schonbaum, G.R.
    Catalases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 8, Academic Press, New York, 1963, 147-225

[EC 1.11.1.6 created 1961, modified 1986, modified 1999, modified 2013]