Information AboutCatalase |
| CATEGORIES ABOUT CATALASE | |
| ec 1.11.1 | |
| antioxidants | |
| hemoproteins | |
| enzymes | |
| SHOPPER'S DELIGHT | |
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Catalase (human 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 6 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. ROLE IN ORGANISMS 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 (40,000,000 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. 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 Acid s 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. Catalase can also oxidize different toxins, such as Formaldehyde , Formic Acid , and Alcohols . In doing so, it uses Hydrogen Peroxide according to the following reaction: H2O2 + H2R → 2H2O + R Again, the exact mechanism of this reaction is not known. Any heavy metal ion (such as Copper cations in Copper(II) Sulfate ) will act as a Noncompetitive Inhibitor on catalase. Also, the poison Cyanide and Curare is a Competitive Inhibitor to catalase, strongly binding to the active site of catalase and stopping the enzyme's action. 3D Protein Structure s 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. SEE ALSO EXTERNAL LINKS
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