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EC 1.1.5.3 Details

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EC number

1.1.5.3

Accepted name

glycerol-3-phosphate dehydrogenase

Reaction

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol

Other name(s)

α-glycerophosphate dehydrogenase, α-glycerophosphate dehydrogenase (acceptor), anaerobic glycerol-3-phosphate dehydrogenase, DL-glycerol 3-phosphate oxidase (misleading), FAD-dependent glycerol-3-phosphate dehydrogenase, FAD-dependent sn-glycerol-3-phosphate dehydrogenase, FAD-GPDH, FAD-linked glycerol 3-phosphate dehydrogenase, FAD-linked L-glycerol-3-phosphate dehydrogenase, flavin-linked glycerol-3-phosphate dehydrogenase, flavoprotein-linked L-glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate cytochrome c reductase (misleading), glycerol phosphate dehydrogenase, glycerol phosphate dehydrogenase (acceptor), glycerol phosphate dehydrogenase (FAD), glycerol-3-phosphate CoQ reductase, glycerol-3-phosphate dehydrogenase (flavin-linked), glycerol-3-phosphate:CoQ reductase, glycerophosphate dehydrogenase, L-3-glycerophosphate-ubiquinone oxidoreductase, L-glycerol-3-phosphate dehydrogenase (ambiguous), L-glycerophosphate dehydrogenase, mGPD, mitochondrial glycerol phosphate dehydrogenase, NAD⁺-independent glycerol phosphate dehydrogenase, pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase, sn-glycerol 3-phosphate oxidase (misleading), sn-glycerol-3-phosphate dehydrogenase, sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase, sn-glycerol-3-phosphate:acceptor 2-oxidoreductase

Systematic name

sn-glycerol 3-phosphate:quinone oxidoreductase

CAS registry number

9001-49-4

Comment

This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD⁺), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD⁺ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ₁₀ as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ₉ [4]. The enzyme is activated by calcium [3].

History

created 1961 as EC 1.1.2.1, transferred 1965 to EC 1.1.99.5, transferred 2009 to EC 1.1.5.3

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.3 With oxygen as acceptor

1.5.3.1 sarcosine oxidase (formaldehyde-forming)

1.5.3.2 N-methyl-L-amino-acid oxidase

1.5.3.3 created 1961, deleted 1972

1.5.3.4 N⁶-methyl-lysine oxidase

1.5.3.5 (S)-6-hydroxynicotine oxidase

1.5.3.6 (R)-6-hydroxynicotine oxidase

1.5.3.7 L-pipecolate oxidase

1.5.3.8 created 1989, deleted 1992

1.5.3.9 created 1989, modified 1999, deleted 2002

1.5.3.10 dimethylglycine oxidase

1.5.3.11 polyamine oxidase

1.5.3.12 dihydrobenzophenanthridine oxidase

1.5.3.13 N¹-acetylpolyamine oxidase

1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)

1.5.3.15 N⁸-acetylspermidine oxidase (propane-1,3-diamine-forming)

1.5.3.16 spermine oxidase

1.5.3.17 non-specific polyamine oxidase

1.5.3.18 L-saccharopine oxidase

1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)

1.5.3.20 N-alkylglycine oxidase

1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)

1.5.3.22 coenzyme F₄₂₀H₂ oxidase

1.5.3.23 glyphosate oxidoreductase

1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)

1.5.3.25 fructosyl amine oxidase (glucosone-forming)

1.5.3.26 fructosyl amine oxidase (fructosamine-forming)

1.5.4 With a disulfide as acceptor

1.5.5 With a quinone or similar compound as acceptor

1.5.7 With an iron-sulfur protein as acceptor

1.5.8 With a flavin or flavoprotein as acceptor

1.5.98 With other, known, physiological acceptors

1.5.99 With unknown physiological acceptors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)