IUBMB Enzyme Nomenclature

EC 1.11.1.6

Accepted name: catalase

Reaction: 2 H2O2 = O2 + 2 H2O

Other name(s): equilase; caperase; optidase; catalase-peroxidase; CAT

Systematic name: hydrogen-peroxide:hydrogen-peroxide oxidoreductase

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: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-05-2

References:

1. Herbert, D. and Pinsent, J. Crystalline bacterial catalase. Biochem. J. 43 (1948) 193-202. [PMID: 16748386]

2. Herbert, D. and Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203-205. [PMID: 16748387]

3. Keilin, D. and Hartree, E.F. Coupled oxidation of alcohol. Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141-159.

4. Kono, Y. and Fridovich, I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J. Biol. Chem. 258 (1983) 6015-6019. [PMID: 6853475]

5. Nicholls, P. and Schonbaum, G.R. Catalases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 147-225.

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


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