Catalase

Catalase
Identifiers
Symbol	Catalase
Pfam	PF00199
InterPro	IPR011614
PROSITE	PDOC00395
SCOP2	7cat / SCOPe / SUPFAM
OPM superfamily	370
OPM protein	3e4w
CDD	cd00328
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

CAT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DGB, 1DGF, 1DGG, 1DGH, 1F4J, 1QQW
Identifiers
Aliases	CAT, catalase
External IDs	OMIM: 115500; MGI: 88271; HomoloGene: 55514; GeneCards: CAT; OMA:CAT - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p13 Start 34,438,934 bp[1] End 34,472,060 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 E2|2 54.43 cM Start 103,284,194 bp[2] End 103,315,505 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in trabecular bone kidney tubule renal medulla jejunal mucosa liver bone marrow right lobe of liver mucosa of ileum skin of hip skin of thigh Top expressed in left lobe of liver blood proximal tubule tunica adventitia of aorta right kidney subcutaneous adipose tissue stroma of bone marrow brown adipose tissue human kidney intercostal muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity aminoacylase activity peroxidase activity metal ion binding oxidoreductase activity, acting on peroxide as acceptor catalase activity antioxidant activity heme binding NADP binding enzyme binding oxidoreductase activity signaling receptor binding identical protein binding Cellular component cytosol Golgi apparatus membrane intracellular membrane-bounded organelle focal adhesion mitochondrial intermembrane space peroxisomal membrane peroxisome plasma membrane peroxisomal matrix endoplasmic reticulum mitochondrion lysosome extracellular exosome extracellular region extracellular space secretory granule lumen ficolin-1-rich granule lumen Biological process response to phenylpropanoid ureteric bud development response to estradiol response to hypoxia response to cadmium ion response to fatty acid kidney development response to inactivity response to hyperoxia cellular response to growth factor stimulus ageing cholesterol metabolic process response to L-ascorbic acid negative regulation of apoptotic process response to ozone response to oxidative stress response to activity protein tetramerization response to vitamin E response to insulin response to vitamin A aerobic respiration response to lead ion positive regulation of NF-kappaB transcription factor activity osteoblast differentiation hydrogen peroxide catabolic process UV protection positive regulation of phosphatidylinositol 3-kinase signaling response to radiation response to light intensity response to ethanol negative regulation of NF-kappaB transcription factor activity triglyceride metabolic process protein homotetramerization response to UV response to toxic substance response to hydrogen peroxide hemoglobin metabolic process positive regulation of cell division cellular oxidant detoxification neutrophil degranulation response to reactive oxygen species cellular response to oxidative stress protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 847 12359 Ensembl ENSG00000121691 ENSMUSG00000027187 UniProt P04040 P24270 RefSeq (mRNA) NM_001752 NM_009804 RefSeq (protein) NP_001743 NP_033934 Location (UCSC) Chr 11: 34.44 – 34.47 Mb Chr 2: 103.28 – 103.32 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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]