Catalase

Catalase
Identifiers
SymbolCatalase
PfamPF00199
InterProIPR011614
PROSITEPDOC00395
SCOP27cat / SCOPe / SUPFAM
OPM superfamily370
OPM protein3e4w
CDDcd00328
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Catalase
Identifiers
EC no.1.11.1.6
CAS no.9001-05-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
CAT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCAT, catalase
External IDsOMIM: 115500; MGI: 88271; HomoloGene: 55514; GeneCards: CAT; OMA:CAT - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001752

NM_009804

RefSeq (protein)

NP_001743

NP_033934

Location (UCSC)Chr 11: 34.44 – 34.47 MbChr 2: 103.28 – 103.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen.[5] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.[6]

Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7,[8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.[9] The pH optimum for other catalases varies between 4 and 11 depending on the species.[10] The optimum temperature also varies by species.[11]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000121691Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027187Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Chelikani P, Fita I, Loewen PC (January 2004). "Diversity of structures and properties among catalases". Cellular and Molecular Life Sciences. 61 (2): 192–208. doi:10.1007/s00018-003-3206-5. hdl:10261/111097. PMC 11138816. PMID 14745498. S2CID 4411482.
  6. ^ Goodsell DS (2004-09-01). "Catalase". Molecule of the Month. RCSB Protein Data Bank. Retrieved 2016-08-23.
  7. ^ Boon EM, Downs A, Marcey D. "Catalase: H2O2: H2O2 Oxidoreductase". Catalase Structural Tutorial Text. Retrieved 2007-02-11.
  8. ^ Maehly AC, Chance B (1954). "The assay of catalases and peroxidases". Methods of Biochemical Analysis. Vol. 1. pp. 357–424. doi:10.1002/9780470110171.ch14. ISBN 978-0-470-11017-1. PMID 13193536.
  9. ^ Aebi H (1984). "Catalase in vitro". Oxygen Radicals in Biological Systems. Methods in Enzymology. Vol. 105. pp. 121–6. doi:10.1016/S0076-6879(84)05016-3. ISBN 978-0-12-182005-3. PMID 6727660.
  10. ^ "EC 1.11.1.6 - catalase". BRENDA: The Comprehensive Enzyme Information System. Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig. Retrieved 2009-05-26.
  11. ^ Toner K, Sojka G, Ellis R. "A Quantitative Enzyme Study; CATALASE". bucknell.edu. Archived from the original on 2000-06-12. Retrieved 2007-02-11.

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