Catalase
FunctionCatalase (CAT) catalyzes the conversion of hydrogen peroxide to water and oxygen. CAT contains porphyrin-heme Fe group which reacts with the hydrogen peroxide. CAT containing Mn are called pseudocatalase (PCAT).[1] Catalase-peroxidase (CAT KatG) is a bifunctional enzyme with both catalase and peroxidase activities. CAT KatG cofactor is a heme group. It provides defense against oxidative stress by reducing hydrogen peroxide. Mutations in CAT KatG can cause resistance to the anti-malarial drug isoniazid (INH).[2] Catalase-phenol oxidase (CATPO) is a heme-containing CAT which shows phenol oxidase activity.[3] StructureCatalase is a tetramer, each polypeptide chain is over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. Coordination of heme in E. coli catalase.[4] Water molecules are shown as red spheres. As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, 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 Tyr357 in the fifth iron ligand, 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 His74 and Asn147 with reaction intermediates.[5] See more details in Ann Taylor/Catalase 3D Structures of catalase
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References
Proteopedia Page Contributors and Editors (what is this?)
Karsten Theis, Michal Harel, Ann Taylor, Alexander Berchansky
