The Enzyme Database

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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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, 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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