Catalase is a long chain iron bond (heme) enzyme, whose functions include catalyzing the decomposition of hydrogen peroxide to water and oxygen. It is highly concentrated in the liver and used by every organ in the body and found in the cellular organelle. An Enzyme protein complex with hematin groups and catalyzes the decomposition of hydrogen peroxide into water and oxygen. Catalase has a secondary role oxidising toxins. Catalase is one of the most potent antioxidant enzymes active in a pH range of 4-9. •
Catalase is a widely occurring enzyme containing four iron atoms in a 500 amino acid protein. Catalase catalyses the conversion of hydrogen peroxide to water and oxygen at rates of up to 6,000,000 molecules per minute. Catalase has a secondary role oxidising toxins including formaldehyde, formic acid and alcohols.
Catalase can also oxidize different toxins, such as formaldehyde, formic acid, and alcohol.
Technicals: 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.
Antagonist: Any heavy metal ion (such as Copper cations in Copper(II) sulfate) will act as a noncompetitive inhibitor on catalase. Also, cyanide and curare are a competitive inhibitors to catalase, strongly binding to the active site of catalase and stopping the enzyme's action.
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