catalase | 1.-.-.- Oxidoreductases | IUPHAR/BPS Guide to PHARMACOLOGY

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catalase

Target not currently curated in GtoImmuPdb

Target id: 2979

Nomenclature: catalase

Family: 1.-.-.- Oxidoreductases

Annotation status:  image of a grey circle Awaiting annotation/under development. Please contact us if you can help with annotation.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 527 11p13 CAT catalase
Mouse - 527 2 E2; 2 54.43 cM Cat catalase
Rat - 527 3q32 Cat catalase
Previous and Unofficial Names
Cas1 | Cas-1
Database Links
BRENDA
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Enzyme Reaction
EC Number: 1.11.1.6
Description Reaction Reference
Conversion of the reactive oxygen species hydrogen peroxide to water and oxygen. 2 H2O2 <=> O2 + 2 H2O

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Activators
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
tectorigenin Ma Activation - - 11
[11]
Description: Activation of catalase in V79-4 cell in culture.
Antibody Comments
Anti-catalase single-domain antibodies were shown to block catalase-mediated H2O2 breakdown in human tumour cells with the effect of reactivating reactive oxygen species-dependent apoptosis [1]. These antibodies inhibited tumour growth in human tumor xenografts, and the effect was strongly synergistic with paclitaxel chemotherapy.
Clinically-Relevant Mutations and Pathophysiology
Disease:  Acatalasemia
Description: A rare autosomal recessive peroxisomal disorder caused by deficient activity of the enzyme, catalase, that was originally identified in patients suffering from ulcerating oral gangrene. different A number of CAT gene mutations that generate enzymes with varying degress of enzymatic deficiency have been identified. Heterozygotes have an intermediate level of catalase in the blood.
Synonyms: acatalasia
catalase deficiency
Takahara disease
OMIM: 614097
Orphanet: ORPHA926
Role: 
Comments: 
References:  4,6-8,10
General Comments
Catalase is a key antioxidant enzyme that protects cells from oxidative stress by neutralising the toxic effects of hydrogen peroxide. It is located in the peroxisomes of nearly all aerobic cells.
As catalase activity is associated with cytoprotective effects [9], it may be a potential molecular target whose pharmacological modulation could mediate anti-apoptotic functions [11]. Catalase has been implicated in many pathophysiological processes of human diseases, including cancer [3,5]. In tumours, cancer cells may be chronically exposed to oxidative stressors such as hydrogen peroxide in the hypoxic tumour microenvironment, and undergo cellular adaptation (redox adaptation, altered expression of antioxidant enzymes) that allows them to maintain proliferative advantage, but also leaves them sensitive to an oxidant insult. Understanding the molecular mechanisms (e.g. transcription factors, genetic, epigenetic, and posttranscriptional processes) controlling catalase expression will aid future development of novel pro-oxidant cancer chemotherapy [2].

References

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1. Bauer G, Motz M. (2016) The Antitumor Effect of Single-domain Antibodies Directed Towards Membrane-associated Catalase and Superoxide Dismutase. Anticancer Res., 36 (11): 5945-5956. [PMID:27793920]

2. Glorieux C, Calderon PB. (2017) Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol. Chem., 398 (10): 1095-1108. [PMID:28384098]

3. Glorieux C, Zamocky M, Sandoval JM, Verrax J, Calderon PB. (2015) Regulation of catalase expression in healthy and cancerous cells. Free Radic. Biol. Med., 87: 84-97. [PMID:26117330]

4. Góth L, Eaton JW. (2000) Hereditary catalase deficiencies and increased risk of diabetes. Lancet, 356 (9244): 1820-1. [PMID:11117918]

5. Góth L, Rass P, Páy A. (2004) Catalase enzyme mutations and their association with diseases. Mol. Diagn., 8 (3): 141-9. [PMID:15771551]

6. Góth L, Shemirani A, Kalmár T. (2000) Anovel catalase mutation (a GA insertion) causes the Hungarian type of acatalasemia. Blood Cells Mol. Dis., 26 (2): 151-4. [PMID:11001624]

7. HAMILTON HB, NEEL JV. (1963) GENETIC HETEROGENEITY IN HUMAN ACATALASIA. Am. J. Hum. Genet., 15: 408-19. [PMID:14097235]

8. Hirono A, Sasaya-Hamada F, Kanno H, Fujii H, Yoshida T, Miwa S. (1995) A novel human catalase mutation (358 T-->del) causing Japanese-type acatalasemia. Blood Cells Mol. Dis., 21 (3): 232-4. [PMID:8673475]

9. Takeuchi A, Miyamoto T, Yamaji K, Masuho Y, Hayashi M, Hayashi H, Onozaki K. (1995) A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase. Cancer Res., 55 (7): 1586-9. [PMID:7882369]

10. Wen JK, Osumi T, Hashimoto T, Ogata M. (1990) Molecular analysis of human acatalasemia. Identification of a splicing mutation. J. Mol. Biol., 211 (2): 383-93. [PMID:2308162]

11. Zhang R, Piao MJ, Oh MC, Park JE, Shilnikova K, Moon YJ, Kim DH, Jung U, Kim IG, Hyun JW. (2016) Protective Effect of an Isoflavone, Tectorigenin, Against Oxidative Stress-induced Cell Death via Catalase Activation. J Cancer Prev, 21 (4): 257-263. [PMID:28053960]

How to cite this page

1.-.-.- Oxidoreductases: catalase. Last modified on 15/12/2017. Accessed on 21/10/2019. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2979.