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Gene Review

CAT  -  catalase

Homo sapiens

Synonyms: Catalase
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Catalase (CAT) is an enzyme which promotes the redox reaction

H2O2 + H2R → 2H2O + R

When R = O2 it converts hydrogen peroxide to water and molecular oxygen.



Disease relevance of CAT


Psychiatry related information on CAT


High impact information on CAT

  • The premier discoveries to emanate from my laboratory have been the sulfite oxidase, the several superoxide dismutases, the manganese catalase, and the catalase/peroxidase [12].
  • The H2O2-degrading enzyme catalase protects cells from A beta toxicity [13].
  • The translocation breakpoint, which identifies the position of the aniridia gene on 11p, is immediately proximal to FSHB, in the interval between FSHB and the catalase gene [14].
  • Previous workers observed that while peroxide was clearly responsible for cytolysis of certain antibody-coated tumour cells, extracellular catalase was unable to inhibit this cytolysis, and they suggested that macrophages secrete peroxide into a protected cleft between the phagocyte and target [15].
  • Catalase, a scavenger of H2O2, and superoxide dismutase (SOD), a scavenger of O-2, either alone or in combination, did not inhibit NK cell activity [16].

Chemical compound and disease context of CAT


Biological context of CAT


Anatomical context of CAT


Associations of CAT with chemical compounds


Physical interactions of CAT

  • Catalase binds Grb2 in tumor cells when stimulated with serum or ligands for integrin receptors [27].
  • SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling [28].
  • Recently, however, mammalian catalase was found to have tightly bound NADPH and to require NADPH for the prevention and reversal of inactivation by its toxic substrate (H2O2) [1].
  • Amyloid-beta (Abeta) specifically bound purified catalase with high affinity and inhibited catalase breakdown of H(2)O(2) [29].
  • Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown [29].

Enzymatic interactions of CAT


Regulatory relationships of CAT


Other interactions of CAT


Analytical, diagnostic and therapeutic context of CAT


  1. Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. Gaetani, G.F., Galiano, S., Canepa, L., Ferraris, A.M., Kirkman, H.N. Blood (1989) [Pubmed]
  2. Active involvement of catalase during hemolytic crises of favism. Gaetani, G.F., Rolfo, M., Arena, S., Mangerini, R., Meloni, G.F., Ferraris, A.M. Blood (1996) [Pubmed]
  3. Polymorphisms in genes related to oxidative stress (MPO, MnSOD, CAT) and survival after treatment for breast cancer. Ambrosone, C.B., Ahn, J., Singh, K.K., Rezaishiraz, H., Furberg, H., Sweeney, C., Coles, B., Trovato, A. Cancer Res. (2005) [Pubmed]
  4. Catalase protects HepG2 cells from apoptosis induced by DNA-damaging agents by accelerating the degradation of p53. Bai, J., Cederbaum, A.I. J. Biol. Chem. (2003) [Pubmed]
  5. UVB light stimulates production of reactive oxygen species: unexpected role for catalase. Heck, D.E., Vetrano, A.M., Mariano, T.M., Laskin, J.D. J. Biol. Chem. (2003) [Pubmed]
  6. Polymorphisms and functional activity in superoxide dismutase and catalase genes in smokers with COPD. Mak, J.C., Ho, S.P., Yu, W.C., Choo, K.L., Chu, C.M., Yew, W.W., Lam, W.K., Chan-Yeung, M. Eur. Respir. J. (2007) [Pubmed]
  7. Antioxidant defense mechanisms of endothelial cells and renal tubular epithelial cells in vitro: role of the glutathione redox cycle and catalase. Andreoli, S.P., Mallett, C., McAteer, J.A., Williams, L.V. Pediatr. Res. (1992) [Pubmed]
  8. Oxidative stress in Rett syndrome. Sierra, C., Vilaseca, M.A., Brandi, N., Artuch, R., Mira, A., Nieto, M., Pineda, M. Brain Dev. (2001) [Pubmed]
  9. Regional brain activity of free radical defense enzymes in autopsy samples from patients with Alzheimer's disease and from nondemented controls. Chen, L., Richardson, J.S., Caldwell, J.E., Ang, L.C. Int. J. Neurosci. (1994) [Pubmed]
  10. Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development. McElroy, M.C., Postle, A.D., Kelly, F.J. Biochim. Biophys. Acta (1992) [Pubmed]
  11. Del11p13/nephroblastoma without aniridia. Turleau, C., de Grouchy, J., Nihoul-Fékété, C., Dufier, J.L., Chavin-Colin, F., Junien, C. Hum. Genet. (1984) [Pubmed]
  12. With the help of giants. Fridovich, I. Annu. Rev. Biochem. (2003) [Pubmed]
  13. Hydrogen peroxide mediates amyloid beta protein toxicity. Behl, C., Davis, J.B., Lesley, R., Schubert, D. Cell (1994) [Pubmed]
  14. The beta-subunit of follicle-stimulating hormone is deleted in patients with aniridia and Wilms' tumour, allowing a further definition of the WAGR locus. Glaser, T., Lewis, W.H., Bruns, G.A., Watkins, P.C., Rogler, C.E., Shows, T.B., Powers, V.E., Willard, H.F., Goguen, J.M., Simola, K.O. Nature (1986) [Pubmed]
  15. Phagocytosing macrophages exclude proteins from the zones of contact with opsonized targets. Wright, S.D., Silverstein, S.C. Nature (1984) [Pubmed]
  16. Hydroxyl radical scavengers inhibit human natural killer cell activity. Suthanthiran, M., Solomon, S.D., Williams, P.S., Rubin, A.L., Novogrodsky, A., Stenzel, K.H. Nature (1984) [Pubmed]
  17. Adenovirus-mediated overexpression of catalase in the cytosolic or mitochondrial compartment protects against toxicity caused by glutathione depletion in HepG2 cells expressing CYP2E1. Marí, M., Bai, J., Cederbaum, A.I. J. Pharmacol. Exp. Ther. (2002) [Pubmed]
  18. Adenosine deaminase, 5'-nucleotidase, xanthine oxidase, superoxide dismutase, and catalase activities in gastric juices from patients with gastric cancer, ulcer, and atrophic gastritis. Durak, I., Ormeci, N., Akyol, O., Canbolat, O., Kavutçu, M., Bülbül, M. Dig. Dis. Sci. (1994) [Pubmed]
  19. Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle. Kar, N.C., Pearson, C.M. Clin. Chim. Acta (1979) [Pubmed]
  20. Enzyme activities and level of SH groups in breast carcinomas. Rzymowska, J., Dyrda, Z. Int. J. Biochem. (1993) [Pubmed]
  21. Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. Yoo, J.H., Erzurum, S.C., Hay, J.G., Lemarchand, P., Crystal, R.G. J. Clin. Invest. (1994) [Pubmed]
  22. Hydrogen peroxide metabolism in human monocytes during differentiation in vitro. Nakagawara, A., Nathan, C.F., Cohn, Z.A. J. Clin. Invest. (1981) [Pubmed]
  23. FOXO transcription factor activation by oxidative stress mediated by the small GTPase Ral and JNK. Essers, M.A., Weijzen, S., de Vries-Smits, A.M., Saarloos, I., de Ruiter, N.D., Bos, J.L., Burgering, B.M. EMBO J. (2004) [Pubmed]
  24. Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient. Stendahl, O., Coble, B.I., Dahlgren, C., Hed, J., Molin, L. J. Clin. Invest. (1984) [Pubmed]
  25. Changes in the localization of catalase during differentiation of neutrophilic granulocytes. Ballinger, C.A., Mendis-Handagama, C., Kalmar, J.R., Arnold, R.R., Kinkade, J.M. Blood (1994) [Pubmed]
  26. Viricidal effect of polymorphonuclear leukocytes on human immunodeficiency virus-1. Role of the myeloperoxidase system. Klebanoff, S.J., Coombs, R.W. J. Clin. Invest. (1992) [Pubmed]
  27. Catalase binds Grb2 in tumor cells when stimulated with serum or ligands for integrin receptors. Yano, S., Arroyo, N., Yano, N. Free Radic. Biol. Med. (2004) [Pubmed]
  28. SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling. Yano, S., Arroyo, N., Yano, N. FEBS Lett. (2004) [Pubmed]
  29. Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Milton, N.G. Biochem. J. (1999) [Pubmed]
  30. Identification of catalase in human livers as a factor that enhances phenytoin dihydroxy metabolite formation by human liver microsomes. Komatsu, T., Yamazaki, H., Nakajima, M., Yokoi, T. Biochem. Pharmacol. (2002) [Pubmed]
  31. pH Profile of cytochrome c-catalyzed tyrosine nitration. Kambayashi, Y., Hitomi, Y., Kodama, N., Kubo, M., Okuda, J., Takemoto, K., Shibamori, M., Takigawa, T., Ogino, K. Acta Biochim. Pol. (2006) [Pubmed]
  32. Catalase and glutathione reductase protection of human alveolar macrophages during oxidant exposure in vitro. Pietarinen, P., Raivio, K., Devlin, R.B., Crapo, J.D., Chang, L.Y., Kinnula, V.L. Am. J. Respir. Cell Mol. Biol. (1995) [Pubmed]
  33. Increase in liver antioxidant enzyme activities in non-alcoholic fatty liver disease. Perlemuter, G., Davit-Spraul, A., Cosson, C., Conti, M., Bigorgne, A., Paradis, V., Corre, M.P., Prat, L., Kuoch, V., Basdevant, A., Pelletier, G., Oppert, J.M., Buffet, C. Liver Int. (2005) [Pubmed]
  34. Catalase regulates cell growth in HL60 human promyelocytic cells: evidence for growth regulation by H(2)O(2). Hachiya, M., Akashi, M. Radiat. Res. (2005) [Pubmed]
  35. Diet supplementation with vitamin E, vitamin C and beta-carotene cocktail enhances basal neutrophil antioxidant enzymes in athletes. Tauler, P., Aguiló, A., Fuentespina, E., Tur, J.A., Pons, A. Pflugers Arch. (2002) [Pubmed]
  36. Direct evidence for catalase as the predominant H2O2 -removing enzyme in human erythrocytes. Mueller, S., Riedel, H.D., Stremmel, W. Blood (1997) [Pubmed]
  37. Enhanced glutathione peroxidase expression protects cells from hydroperoxides but not from radiation or doxorubicin. Liebmann, J., Fisher, J., Lipschultz, C., Kuno, R., Kaufman, D.C. Cancer Res. (1995) [Pubmed]
  38. Cytochrome P450 2E1 responsiveness in the promoter of glutamate-cysteine ligase catalytic subunit. Nieto, N., Marí, M., Cederbaum, A.I. Hepatology (2003) [Pubmed]
  39. Control of ceramide-induced apoptosis by IGF-1: involvement of PI-3 kinase, caspase-3 and catalase. Kondo, T., Kitano, T., Iwai, K., Watanabe, M., Taguchi, Y., Yabu, T., Umehara, H., Domae, N., Uchiyama, T., Okazaki, T. Cell Death Differ. (2002) [Pubmed]
  40. Vitamin D is a prooxidant in breast cancer cells. Koren, R., Hadari-Naor, I., Zuck, E., Rotem, C., Liberman, U.A., Ravid, A. Cancer Res. (2001) [Pubmed]
  41. Effects of recombinant human extracellular-superoxide dismutase type C on myocardial infarct size in pigs. Hatori, N., Sjöquist, P.O., Marklund, S.L., Rydén, L. Free Radic. Biol. Med. (1992) [Pubmed]
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