Catalase - wikipedia Catalase Catalase Identifiers Symbol Catalase Pfam PF00199 InterPro IPR011614 PROSITE PDOC00395 SCOP 7cat SUPERFAMILY 7cat OPM superfamily 435 OPM protein 3e4w CDD cd00328 Available protein structures : Pfam structures PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary Catalase Identifiers EC number 1.11. 1.6 CAS number 9001 - 05 - 2 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO Search PMC articles PubMed articles NCBI proteins 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 MGI : 88271 HomoloGene : 55514 GeneCards : CAT Gene location ( Human ) Chr. Chromosome 11 ( human ) Band 11p13 Start 34,438,925 bp End 34,472,062 bp Gene location ( Mouse ) Chr. Chromosome 2 ( mouse ) Band 2 E2 2 54.43 cM Start 103,453,849 bp End 103,485,160 bp RNA expression pattern 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 receptor 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 aging 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 oxidation - reduction process triglyceride metabolic process protein homotetramerization response to UV response to toxic substance response to hydrogen peroxide response to drug hemoglobin metabolic process positive regulation of cell division cellular oxidant detoxification neutrophil degranulation response to reactive oxygen species cellular response to oxidative stress 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 11 : 103.45 -- 103.49 Mb PubMed search 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 ). It catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species ( ROS ). Likewise, 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. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four iron - containing heme groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for human catalase is approximately 7, and has a fairly broad maximum : the rate of reaction does not change appreciably between pH 6.8 and 7.5. The pH optimum for other catalases varies between 4 and 11 depending on the species. The optimum temperature also varies by species. Contents 1 Structure 2 History 3 Function 3.1 Action 3.2 Molecular mechanism 3.3 Cellular role 4 Distribution among organisms 5 Clinical significance and application 5.1 Bacterial identification ( catalase test ) 5.2 Bacterial virulence 5.3 Gray hair 6 Interactions 7 See also 8 References 9 External links Structure Human catalase forms a tetramer composed of four subunits, each of which can be conceptually divided into four domains. The extensive core of each subunit is generated by an eight - stranded antiparallel b - barrel ( b1 - 8 ), with nearest neighbor connectivity capped by b - barrel loops on one side and a9 loops on the other. A helical domain at one face of the b - barrel is composed of four C - terminal helices ( a16, a17, a18, and a19 ) and four helices derived from residues between b4 and b5 ( a4, a5, a6, and a7 ). Alternative splicing may result in different protein variants. History Catalase was not noticed until 1818 when Louis Jacques Thénard, who discovered H O ( hydrogen peroxide ), suggested its breakdown is caused by an unknown substance. In 1900, Oscar Loew was the first to give it the name catalase, and found it in many plants and animals. In 1937 catalase from beef liver was crystallised by James B. Sumner and Alexander Dounce and the molecular weight was found in 1938. The amino acid sequence of bovine catalase was determined in 1969, and the three - dimensional structure in 1981. Function Action Catalase catalyzes the following reaction : 2 H O → 2 H O + O The presence of catalase in a microbial or tissue sample can be demonstrated by adding hydrogen peroxide and observing the reaction. The production of oxygen can be seen by the formation of bubbles. This easy test, which can be seen with the naked eye, without the aid of instruments, is possible because catalase has a very high specific activity, which produces a detectable response, as well as the fact that one of the products is a gas. Molecular mechanism While the complete mechanism of catalase is not currently known, the reaction is believed to occur in two stages : H O + Fe ( III ) - E → H O + O = Fe ( IV ) - E (. + ) H O + O = Fe ( IV ) - E (. + ) → H O + Fe ( III ) - E + O Here Fe ( ) - E represents the iron center of the heme group attached to the enzyme. Fe ( IV ) - E (. + ) is a mesomeric form of Fe ( V ) - E, meaning the iron is not completely oxidized to + V, but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation (. + ). As hydrogen peroxide enters the active site, it interacts with the amino acids Asn148 ( asparagine at position 148 ) and His75, causing a proton ( hydrogen ion ) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe ( IV ) = O. Fe ( IV ) = O reacts with a second hydrogen peroxide molecule to reform Fe ( III ) - E and produce water and oxygen. The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr358 in the fifth coordination position, which can assist in the oxidation of the Fe ( III ) to Fe ( IV ). The efficiency of the reaction may also be improved by the interactions of His75 and Asn148 with reaction intermediates. In general, the rate of the reaction can be determined by the Michaelis - Menten equation. Catalase can also catalyze the oxidation, by hydrogen peroxide, of various metabolites and toxins, including formaldehyde, formic acid, phenols, acetaldehyde and alcohols. It does so according to the following reaction : H O + H R → 2H O + R The exact mechanism of this reaction is not known. Any heavy metal ion ( such as copper cations in copper ( II ) sulfate ) can act as a noncompetitive inhibitor of catalase. Furthermore, the poison cyanide is a competitive inhibitor of catalase at high concentrations of hydrogen peroxide. Arsenate acts as an activator. Three - dimensional protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank. Cellular role Hydrogen peroxide is a harmful byproduct of many normal metabolic processes ; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the decomposition of hydrogen peroxide into less - reactive gaseous oxygen and water molecules. Mice genetically engineered to lack catalase are initially phenotypically normal., however, catalase deficiency in mice may increase the likelihood of developing obesity, fatty liver, and type 2 diabetes. Some humans have very low levels of catalase ( acatalasia ), yet show few ill effects. Catalase is usually located in a cellular organelle called the peroxisome. Peroxisomes in plant cells are involved in photorespiration ( the use of oxygen and production of carbon dioxide ) and symbiotic nitrogen fixation ( the breaking apart of diatomic nitrogen ( N ) to reactive nitrogen atoms ). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase - positive pathogens, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the host. Like alcohol dehydrogenase, catalase converts ethanol to acetaldehyde, but it is unlikely that this reaction is physiologically significant. Distribution among organisms The large majority of known organisms use catalase in every organ, with particularly high concentrations occurring in the liver in mammals. One unique use of catalase occurs in the bombardier beetle. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains hydroquinones and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and peroxidases. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant. The oxidation reaction is very exothermic ( ΔH = − 202.8 kJ / mol ) and rapidly heats the mixture to the boiling point. Almost all aerobic microorganisms use catalase. It is also present in some anaerobic microorganisms, such as Methanosarcina barkeri. Catalase is also universal among plants and occurs in most fungi. Catalase enzymes from various species have vastly differing optimum temperatures. Poikilothermic animals typically have catalases with optimum temperatures in the range of 15 - 25 ° C, while mammalian or avian catalases might have optimum temperatures above 35 ° C, and catalases from plants vary depending on their growth habit. In contrast, catalase isolated from the hyperthermophile archaeon Pyrobaculum calidifontis has a temperature optimum of 90 ° C. Clinical significance and application Hydrogen peroxide Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production. Another use is in food wrappers where it prevents food from oxidizing. Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide - free. A minor use is in contact lens hygiene -- a few lens - cleaning products disinfect the lens using a hydrogen peroxide solution ; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again. Bacterial identification ( catalase test ) Positive catalase reaction The catalase test is one of the three main tests used by microbiologists to identify species of bacteria. If the bacteria possess catalase ( i.e., are catalase - positive ), when a small amount of bacterial isolate is added to hydrogen peroxide, bubbles of oxygen are observed. The catalase test is done by placing a drop of hydrogen peroxide on a microscope slide. An applicator stick is touched to the colony, and the tip is then smeared onto the hydrogen peroxide drop. If the mixture produces bubbles or froth, the organism is said to be ' catalase - positive '. Staphylococci and Micrococci are catalase - positive. Other catalase - positive organisms include Listeria, Corynebacterium diphtheriae, Burkholderia cepacia, Nocardia, the family Enterobacteriaceae ( Citrobacter, E. coli, Enterobacter, Klebsiella, Shigella, Yersinia, Proteus, Salmonella, Serratia ), Pseudomonas, Mycobacterium tuberculosis, Aspergillus, Cryptococcus, and Rhodococcus equi. If not, the organism is ' catalase - negative '. Streptococcus and Enterococcus spp. are catalase - negative. While the catalase test alone can not identify a particular organism, it can aid identification when combined with other tests such as antibiotic resistance. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells. Capillary tubes may also be used. A small sample of bacteria is collected on the end of the capillary tube, without blocking the tube, to avoid false negative results. The opposite end is then dipped into hydrogen peroxide, which is drawn into the tube through capillary action, and turned upside down, so that the bacterial points downwards. The hand holding the tube is then tapped on the bench, moving the hydrogen peroxide down until it touches the bacteria. If bubbles form on contact, this indicates a positive catalase result. This test can detect catalase - positive bacteria at concentrations above about 10 cells / mL, and is simple to use. Bacterial virulence Neutrophils and other phagocytes use peroxide to kill bacteria. The enzyme NADPH oxidase generates superoxide within the phagosome, which is converted via hydrogen peroxide to other oxidising substances like hypochlorous acid which kill phagocytosed pathogens. In individuals with chronic granulomatous disease ( CGD ) there is a defect in producing peroxide via mutations in phagocyte oxidases such as myeloperoxidase. Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase - positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a granuloma. Many bacteria are catalase positive, but some are better catalase - producers than others. The mnemonic `` cats Need PLACESS to Belch their Hairballs '' can be used to memorise the catalase - positive bacteria : nocardia, pseudomonas, listeria, aspergillus, candida, E. coli, staphylococcus, serratia, B. cepacia and H. pylori. Gray hair Low levels of catalase may play a role in the graying process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide can not be broken down so well. The hydrogen peroxide interferes with the production of melanin, the pigment that gives hair its color. Interactions Catalase has been shown to interact with the ABL2 and Abl genes. Infection with the murine leukemia virus causes catalase activity to decline in the lungs, heart and kidneys of mice. Conversely, dietary fish oil increased catalase activity in the heart, and kidneys of mice. 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MadSci FAQ. madsci.org. Retrieved 2009 - 03 - 05. `` Catalase and oxidase test video ''. Regnvm Prokaryotae. Retrieved 2009 - 03 - 05. `` EC 1.11. 1.6 - catalase ''. Brenda : The Comprehensive Enzyme Information System. Retrieved 2009 - 03 - 05. `` PeroxiBase - The peroxidase database ''. Swiss Institute of Bioinformatics. Archived from the original on 2008 - 10 - 13. Retrieved 2009 - 03 - 05. `` Catalase Procedure ''. MicrobeID.com. Retrieved 2009 - 04 - 22. `` Catalase Molecule of the Month ''. Protein Data Bank. Archived from the original on 2013 - 05 - 11. Retrieved 2013 - 01 - 08. Peroxisomal and lysosomal proteins Enzymes Mevalonate kinase Catalase Acetyl - CoA C - acyltransferase Glyceronephosphate O - acyltransferase Alkylglycerone phosphate synthase Phytanoyl - CoA dioxygenase HSD17B4 AMACR Transporters SLC27A2 Structure / Peroxin PEX1 PXMP3 PEX3 PEX5 PEX6 PEX7 PEX10 PEX11A PEX11B PEX11G PEX12 PEX13 PEX14 PEX16 PEX19 PEX26 LAMP CD68 LAMP1 LAMP2 LAMP3 see also intermediates, disorders Oxidoreductases : peroxidases ( EC 1.11 ) 1.11. 1.1 - 14 Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase 1.11. 1.15 ( peroxiredoxin ) 5 6 Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics Types EC1 Oxidoreductases ( list ) EC2 Transferases ( list ) EC3 Hydrolases ( list ) EC4 Lyases ( list ) EC5 Isomerases ( list ) EC6 Ligases ( list ) Molecular and Cellular Biology portal Retrieved from `` https://en.wikipedia.org/w/index.php?title=Catalase&oldid=813550950 '' Categories : Genes on human chromosome 11 EC 1.11. 1 Antioxidants Hemoproteins Enzymes Catalysis Talk Search Contents About Wikipedia Afrikaans تۆرکجه Bosanski Català Čeština Dansk Deutsch Español Euskara فارسی Français Galego 한국어 Հայերեն Hrvatski Ido Bahasa Indonesia Italiano עברית ಕನ್ನಡ Bahasa Melayu Nederlands 日本 語 Norsk Norsk nynorsk Polski Português Română Русский Slovenščina Српски / srpski Srpskohrvatski / српскохрватски Svenska Türkçe Українська 中文 Edit links This page was last edited on 4 December 2017, at 01 : 10. 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Question: where do you find catalase in the body
Answer: in every organ, with particularly high concentrations occurring in the liver in mammals