catalase

Target not currently curated in GtoImmuPdb

Target id: 2979

Nomenclature: catalase

Gene and Protein Information
Species	TM	AA	Chromosomal Location	Gene Symbol	Gene Name	Reference
Human	-	527	11p13	CAT	catalase
Mouse	-	527	2 54.43 cM	Cat	catalase
Rat	-	527	3q32	Cat	catalase

Previous and Unofficial Names
Cas1 \| Cas-1

Database Links
Alphafold	P04040 (Hs), P24270 (Mm), P04762 (Rn)
BRENDA	1.11.1.6
ChEMBL Target	CHEMBL3627594 (Hs), CHEMBL1075216 (Rn)
DrugBank Target	CHEMBL1075216 (Rn)
Ensembl Gene	ENSG00000121691 (Hs), ENSMUSG00000027187 (Mm), ENSRNOG00000008364 (Rn)
Entrez Gene	847 (Hs), 12359 (Mm), 24248 (Rn)
Human Protein Atlas	ENSG00000121691 (Hs)
KEGG Enzyme	1.11.1.6
KEGG Gene	hsa:847 (Hs), mmu:12359 (Mm), rno:24248 (Rn)
OMIM	115500 (Hs)
Pharos	P04040 (Hs)
RefSeq Nucleotide	NM_001752 (Hs), NM_009804 (Mm), NM_012520 (Rn)
RefSeq Protein	NP_001743 (Hs), NP_033934 (Mm), NP_036652 (Rn)
UniProtKB	P04040 (Hs), P24270 (Mm), P04762 (Rn)
Wikipedia	CAT (Hs)

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

Download all structure-activity data for this target as a CSV file go icon to follow link

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.

Immuno Process Associations

Immuno Process:

Inflammation

Immuno Process:

Cellular signalling

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:

Patients with acatalasemia are unable to breakdown hydrogen peroxide, leaving their tissues at risk of oxidative damage. Patients may be asymptomatic, but symptoms can include progressive oral gangrene. Acatalasemia is associated with diabetes mellitus and atherosclerosis in some defined populations.

Comments:

Genetic heterogeneity is found in patients with acatalasemia.

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].

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

Show »« Hide

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 16/04/2024. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2979.

catalase

Contents:

References

How to cite this page