| 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. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 147–225. |
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| [EC 1.11.1.6 created 1961, modified 1986, modified 1999, modified 2013] |
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