Glycerol-3-phosphate oxidase

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glycerol-3-phosphate oxidase
Identifiers
EC no. 1.1.3.21
CAS no. 9046-28-0
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In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction

sn-glycerol 3-phosphate + O2 glycerone phosphate + H2O2

Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are dihydroxyacetone phosphate (DHAP) 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 sn-glycerol-3-phosphate:oxygen 2-oxidoreductase. Other names in common use include glycerol phosphate oxidase, glycerol-1-phosphate oxidase, glycerol phosphate oxidase, L-alpha-glycerophosphate oxidase, alpha-glycerophosphate oxidase, and L-alpha-glycerol-3-phosphate oxidase. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.

Related Research Articles

<span class="mw-page-title-main">Glycerol phosphate shuttle</span> NADH transport mechanism in mitochondria

The glycerol-3-phosphate shuttle is a mechanism used in skeletal muscle and the brain that regenerates NAD+ from NADH, a by-product of glycolysis. NADH is a reducing equivalent that stores electrons generated in the cytoplasm during glycolysis. NADH must be transported into the mitochondria to enter the oxidative phosphorylation pathway. However, the inner mitochondrial membrane is impermeable to NADH and only contains a transport system for NAD+. Depending on the type of tissue either the glycerol-3-phosphate shuttle pathway or the malate–aspartate shuttle pathway is used to transport electrons from cytoplasmic NADH into the mitochondria.

<span class="mw-page-title-main">Glycerol-3-phosphate dehydrogenase</span> Class of enzymes

Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate to sn-glycerol 3-phosphate.

<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 hydroxylated 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.

Glycerol-3-phosphate dehydrogenase (NAD<sup>+</sup>)

In enzymology, a glycerol-3-phosphate dehydrogenase (NAD+) (EC 1.1.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a hexose oxidase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Pyranose oxidase</span>

In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a pyridoxine 4-oxidase (EC 1.1.3.12) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">(S)-2-hydroxy-acid oxidase</span> Class of enzymes

In enzymology, an (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) is an enzyme that catalyzes the chemical reaction

In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Oxalate oxidase</span>

In enzymology, an oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:

In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Amine oxidase (copper-containing)</span> Protein domain

Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:

In enzymology, a L-aspartate oxidase (EC 1.4.3.16) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-pipecolate oxidase (EC 1.5.3.7) is an enzyme that catalyzes the chemical reaction

In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction

In enzymology, a glycerol-3-phosphate O-acyltransferase is an enzyme that catalyzes the chemical reaction

References


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