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Primary Information | |
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| BoMiProt ID | Bomi4508 |
| Protein Name | Catalase |
| Organism | Bos taurus |
| Uniprot ID | P00432 |
| Milk Fraction | Exosomes |
| Ref Sequence ID | NP_001030463.1 |
| Aminoacid Length | 527 |
| Molecular Weight | 59915 |
| FASTA Sequence | Download |
| Gene Name | CAT |
| Gene ID | 531682 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | liver |
| Protein Function | Catalase is a key enzyme in the metabolism of H2O2 and reactive nitrogen species, and its expression and localization is markedly altered in tumors. |
| Biochemical Properties | Human catalase contains four identical subunits of 62 kDa, each subunit containing four distinct domains and one prosthetic heme group. The four domains include: (1) a N-terminal arm which contains a distal histidine, an essential amino acid for the catalase reaction; (2) a β-barrel domain that contains eight β-barrels arranged in an antiparallel fashion with six α-helical insertions, conferring the hydrophobic core of the protein necessary for the tri-dimensional structure of the enzyme; (3) a connection domain which contains the tyrosine residue that binds the heme group; and finally (4) an α-helical domains, which is important for NADPH binding. |
| PTMs | N6-Acetylation at Lys, Phosphorylation at Ser |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P00432|CATA_BOVIN Catalase OS=Bos taurus OX=9913 GN=CAT PE=1 SV=3 MADNRDPAS*9DQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDE MAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGES GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPD MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ GIKNLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLT KVWPHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPD THRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPS*417ALE HRTHFSGDVQRFNS*434ANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVK NFSDVHPEYGSRIQALLDKYNEEKPKNAVHT*511YVQHGS*517HLSAREKANL |
| SCOP | Class : All beta proteins Fold : Streptavidin-like Superfamily : Heme-dependent catalase-like Family : Heme-dependent catalases Domain Name : 4BLC A:3-501 |
| CATH | Matched CATH superfamily 1.10.8.1230 1.20.1370.60 2.40.180.20 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 1TGU, 1TH2, 1TH3, 1TH4, 3J7B, 3NWL, 3RE8, 3RGP, 3RGS, 4BLC, 5GKN, 6JNT, 6JNU, 6PM7, 6PO0, 7CAT, 7DI8, 8CAT, |
| Bibliography | 1.Glorieux C, Calderon PB. Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol Chem. 2017 Sep 26;398(10):1095-1108. doi: 10.1515/hsz-2017-0131. PMID: 28384098. 2.Nagem, R.A., Martins, E.A., Goncalves, V.M., Aparicio, R., and Polikarpov, I. (1999). Crystallization and preliminary X-ray diffraction studies of human catalase. Acta Crystallogr. D Biol. Crystallogr. 55, 1614–1615.10.1107/S0907444999009695. 3.Zamocky, M. and Koller, F. (1999). Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol. 72, 19–66.10.1016/S0079-6107(98)00058-3. 4.Putnam, C.D., Arvai, A.S., Bourne, Y., and Tainer, J.A. (2000). Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296, 295–309.10.1006/jmbi.1999.3458. |