Catalase
Details
- Name
- Catalase
- Kind
- protein
- Synonyms
- 1.11.1.6
- Gene Name
- CAT
- UniProtKB Entry
- P04040Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0020512|Catalase MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
- Number of residues
- 527
- Molecular Weight
- 59755.82
- Theoretical pI
- 7.41
- GO Classification
- Functionsidentical protein bindingProcessescellular detoxification of hydrogen peroxide / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to xenobiotic stimulusComponentscatalase complex / cytoplasm / extracellular region / ficolin-1-rich granule lumen / protein-containing complex / secretory granule lumen
- General Function
- Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369)
- Specific Function
- aminoacylase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Peroxisome matrix
- Gene sequence
>lcl|BSEQ0020513|Catalase (CAT) ATGGCTGACAGCCGGGATCCCGCCAGCGACCAGATGCAGCACTGGAAGGAGCAGCGGGCC GCGCAGAAAGCTGATGTCCTGACCACTGGAGCTGGTAACCCAGTAGGAGACAAACTTAAT GTTATTACAGTAGGGCCCCGTGGGCCCCTTCTTGTTCAGGATGTGGTTTTCACTGATGAA ATGGCTCATTTTGACCGAGAGAGAATTCCTGAGAGAGTTGTGCATGCTAAAGGAGCAGGG GCCTTTGGCTACTTTGAGGTCACACATGACATTACCAAATACTCCAAGGCAAAGGTATTT GAGCATATTGGAAAGAAGACTCCCATCGCAGTTCGGTTCTCCACTGTTGCTGGAGAATCG GGTTCAGCTGACACAGTTCGGGACCCTCGTGGGTTTGCAGTGAAATTTTACACAGAAGAT GGTAACTGGGATCTCGTTGGAAATAACACCCCCATTTTCTTCATCAGGGATCCCATATTG TTTCCATCTTTTATCCACAGCCAAAAGAGAAATCCTCAGACACATCTGAAGGATCCGGAC ATGGTCTGGGACTTCTGGAGCCTACGTCCTGAGTCTCTGCATCAGGTTTCTTTCTTGTTC AGTGATCGGGGGATTCCAGATGGACATCGCCACATGAATGGATATGGATCACATACTTTC AAGCTGGTTAATGCAAATGGGGAGGCAGTTTATTGCAAATTCCATTATAAGACTGACCAG GGCATCAAAAACCTTTCTGTTGAAGATGCGGCGAGACTTTCCCAGGAAGATCCTGACTAT GGCATCCGGGATCTTTTTAACGCCATTGCCACAGGAAAGTACCCCTCCTGGACTTTTTAC ATCCAGGTCATGACATTTAATCAGGCAGAAACTTTTCCATTTAATCCATTCGATCTCACC AAGGTTTGGCCTCACAAGGACTACCCTCTCATCCCAGTTGGTAAACTGGTCTTAAACCGG AATCCAGTTAATTACTTTGCTGAGGTTGAACAGATAGCCTTCGACCCAAGCAACATGCCA CCTGGCATTGAGGCCAGTCCTGACAAAATGCTTCAGGGCCGCCTTTTTGCCTATCCTGAC ACTCACCGCCATCGCCTGGGACCCAATTATCTTCATATACCTGTGAACTGTCCCTACCGT GCTCGAGTGGCCAACTACCAGCGTGACGGCCCGATGTGCATGCAGGACAATCAGGGTGGT GCTCCAAATTACTACCCCAACAGCTTTGGTGCTCCGGAACAACAGCCTTCTGCCCTGGAG CACAGCATCCAATATTCTGGAGAAGTGCGGAGATTCAACACTGCCAATGATGATAACGTT ACTCAGGTGCGGGCATTCTATGTGAACGTGCTGAATGAGGAACAGAGGAAACGTCTGTGT GAGAACATTGCCGGCCACCTGAAGGATGCACAAATTTTCATCCAGAAGAAAGCGGTCAAG AACTTCACTGAGGTCCACCCTGACTACGGGAGCCACATCCAGGCTCTTCTGGACAAGTAC AATGCTGAGAAGCCTAAGAATGCGATTCACACCTTTGTGCAGTCCGGATCTCACTTGGCG GCAAGGGAGAAGGCAAATCTGTGA
- Chromosome Location
- 11
- Locus
- 11p13
- External Identifiers
Resource Link UniProtKB ID P04040 UniProtKB Entry Name CATA_HUMAN GenBank Protein ID 1228085 GenBank Gene ID X04085 GeneCard ID CAT GenAtlas ID CAT HGNC ID HGNC:1516 PDB ID(s) 1DGB, 1DGF, 1DGG, 1DGH, 1F4J, 1QQW, 7P8W, 7VD9, 8EL9, 8HID, 8PVD, 8SGV KEGG ID hsa:847 NCBI Gene ID 847 - General References
- Quan F, Korneluk RG, Tropak MB, Gravel RA: Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986 Jul 11;14(13):5321-35. [Article]
- Bell GI, Najarian RC, Mullenbach GT, Hallewell RA: cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561-2. [Article]
- Jin LH, Bahn JH, Eum WS, Kwon HY, Jang SH, Han KH, Kang TC, Won MH, Kang JH, Cho SW, Park J, Choi SY: Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic Biol Med. 2001 Dec 1;31(11):1509-19. [Article]
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- Yoo JH, Erzurum SC, Hay JG, Lemarchand P, Crystal RG: Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. J Clin Invest. 1994 Jan;93(1):297-302. [Article]
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- Takeuchi A, Miyamoto T, Yamaji K, Masuho Y, Hayashi M, Hayashi H, Onozaki K: A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase. Cancer Res. 1995 Apr 1;55(7):1586-9. [Article]
- Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819-23. [Article]
- Wen JK, Osumi T, Hashimoto T, Ogata M: Molecular analysis of human acatalasemia. Identification of a splicing mutation. J Mol Biol. 1990 Jan 20;211(2):383-93. [Article]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [Article]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
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- Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ: Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. [Article]
- Putnam CD, Arvai AS, Bourne Y, Tainer JA: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. [Article]
- Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP: Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Fomepizole approved, vet_approved yes target inhibitor Details Calcium carbimide approved, withdrawn no enzyme substrate Details Hydrogen peroxide approved, vet_approved unknown enzyme substrate Details Cannabidiol approved, investigational unknown target inhibitor Details Medical Cannabis experimental, investigational unknown target inhibitor Details Nabiximols investigational unknown target inhibitor Details Benzoyl peroxide approved unknown enzyme substrate Details Benzoyl peroxide approved unknown target inhibitor Details