Pyridoxine 4-oxidase

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pyridoxine 4-oxidase
Identifiers
EC no. 1.1.3.12
CAS no. 37250-82-1
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In enzymology, a pyridoxine 4-oxidase (EC 1.1.3.12) is an enzyme that catalyzes the chemical reaction

pyridoxine + O2 pyridoxal + H2O2

Thus, the two substrates of this enzyme are pyridoxine and O2, whereas its two products are pyridoxal and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxine:oxygen 4-oxidoreductase. Other names in common use include pyridoxin 4-oxidase, and pyridoxol 4-oxidase. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.

Related Research Articles

Vitamin B<sub>6</sub> Class of chemically related vitamins

Vitamin B6 is one of the B vitamins, and thus an essential nutrient. The term refers to a group of six chemically similar compounds, i.e., "vitamers", which can be interconverted in biological systems. Its active form, pyridoxal 5′-phosphate, serves as a coenzyme in more than 140 enzyme reactions in amino acid, glucose, and lipid metabolism.

<span class="mw-page-title-main">Pyridoxine 5′-phosphate oxidase</span> Class of enzymes

Pyridoxine 5′-phosphate oxidase is an enzyme, encoded by the PNPO gene, that catalyzes several reactions in the vitamin B6 metabolism pathway. Pyridoxine 5′-phosphate oxidase catalyzes the final, rate-limiting step in vitamin B6 metabolism, the biosynthesis of pyridoxal 5′-phosphate, the biologically active form of vitamin B6 which acts as an essential cofactor. Pyridoxine 5′-phosphate oxidase is a member of the enzyme class oxidases, or more specifically, oxidoreductases. These enzymes catalyze a simultaneous oxidation-reduction reaction. The substrate oxidase enzymes is hydroxlyated by one oxygen atom of molecular oxygen. Concurrently, the other oxygen atom is reduced to water. Even though molecular oxygen is the electron acceptor in these enzymes' reactions, they are unique because oxygen does not appear in the oxidized product.

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References