Mixed function oxidase


A mixed-function oxidase is an oxidase that catalyzes a chemical reaction involving an O2 dioxygen molecule, each of which has different oxygen atoms in the reaction. Monooxygenases and hydroxylases are mixed function oxidases.

Oxidases form a family of enzymes that use oxygen as an electron acceptor without the oxygen atoms appearing in the oxidized product. Oxygen is usually reduced to H2O - this is the case with cytochrome c oxidase of the mitochondrial respiratory chain - or hydrogen peroxide H2O2 - as with peroxisome acyl-CoA oxidase. Most oxidases are flavoproteins.

The name "mixed function oxidase" indicates that the enzyme oxidizes two substrates simultaneously. The desaturation of fatty acids in vertebrates is an example of a reaction involving mixed-function oxidase, in which a saturated chain acyl-CoA and a molecule of NADPH are oxidized by an O2 oxygen molecule producing a molecule. monounsaturated chain acyl-CoA, one molecule of NADP and two water molecules. Notes and edit the code

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