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| align="center" colspan="2" |
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| colspan="2" bgcolor="#dddddd" | Identifiers
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| bgcolor="#e7dcc3" | Symbol(s)
| bgcolor="#eeeeee" | [CAT]
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| bgcolor="#e7dcc3" | Entrez
| bgcolor="#eeeeee" | [847]
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| bgcolor="#e7dcc3" | OMIM
| bgcolor="#eeeeee" | [115500]
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| bgcolor="#e7dcc3" | RefSeq
| bgcolor="#eeeeee" | [NM_001752]
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| bgcolor="#e7dcc3" | UniProt
| bgcolor="#eeeeee" | [P04040]
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| bgcolor="#e7dcc3" | PDB
| bgcolor="#eeeeee" | []
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| colspan="2" bgcolor="#dddddd" | Other data
|- class="hiddenStructure"
| bgcolor="#e7dcc3" | EC number
| bgcolor="#eeeeee" | [1.11.1.6]
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| bgcolor="#e7dcc3" | Locus
| bgcolor="#eeeeee" | Chr. 11[p13]
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Catalase (human erythrocyte catalase: PDB [1DGF], EC [1.11.1.6]) is a common enzyme found in living organisms. Its functions include catalyzing the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover rates for all enzymes; one molecule of catalase can convert 5 million molecules of hydrogen peroxide to water and oxygen each minute. Catalase is a tetramer of 4 polypeptide chains which are at least 500 amino acids in length. Within this tetramer there are 4 porphyrin haem (iron) groups which are what allows it to react with the hydrogen peroxide. Its optimum pH is at a neutral level.
The catalase test is done by placing a drop of hydrogen peroxide on a slide. Using an applicator stick, touch the colony and then smear into the hydrogen peroxide. If bubbles form, the organism is catalase positive (staphylococci) and if no bubbles appear, then the organism is catalase negative (streptococci).
Hydrogen peroxide is formed as a waste product of metabolism in many living organisms. It is toxic and must be quickly converted into other, less dangerous, chemicals. To manage this problem, the enzyme catalase is frequently used to rapidly catalyse the decomposition of hydrogen peroxide into harmless oxygen.
Catalase has one of the highest turnover numbers for all known enzymes (500,000 molecules/second)
Role in Pathogenesis
Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Pathogens that are catalase positive make catalase in order to deactivate the peroxide radicals, thus allowing them to survive unharmed in the host cell.
The reaction of catalase in the decomposition of hydrogen peroxide is 2 H2O2 → 2 H2O + O2.
Human Applications
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 - some lens-cleaning systems disinfect the lenses by soaking them in a hydrogen peroxide solution, and catalase is used to decompose the peroxide before reinserting the lenses in the eye. Recently, catalase has begun to be used in the aesthetics industry in mask treatments combining the enzyme with hydrogen peroxide on the face to increase cellular oxygenation of cells in the upper layers of the epidermis.
Molecular Mechanism
The complete mechanism of catalase is not yet known; however, the reaction occurs in two stages:
H2O2 + Fe(III)-E → H2O + O=Fe(IV)-E
H2O2 + O=Fe(IV)-E → H2O + Fe(III)-E + O2
(Where Fe-E represents the iron centre of the heme group attached to the enzyme.)
As hydrogen peroxide enters the active site it is forced to interact with the amino acids His74 and Asn174. This causes a proton (hydrogen ion) to transfer from the first oxygen to the second, polarizing and stretching the O-O bond, which breaks heterolytically. The free oxygen atom coordinates with the iron centre of the active site, displacing the newly formed water molecule and forming Fe(IV)=O. In the second stage, the Fe(IV)=O reacts with another hydrogen peroxide to reform Fe(III)-E plus water and oxygen molecules.
3D protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank. This enzyme is commonly used in laboratories as a tool for learning the effect of enzymes upon reaction rates.
