EC - Glycerol-3-phosphate dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
glycerol-3-phosphate dehydrogenase
Other names:
α-glycerophosphate dehydrogenase
α-glycerophosphate dehydrogenase (acceptor)
sn-glycerol 3-phosphate oxidase [misleading]
sn-glycerol-3-phosphate dehydrogenase
DL-glycerol 3-phosphate oxidase [misleading]
L-3-glycerophosphate-ubiquinone oxidoreductase
L-glycerol-3-phosphate dehydrogenase [ambiguous]
L-glycerophosphate dehydrogenase
FAD-dependent sn-glycerol-3-phosphate dehydrogenase
FAD-dependent glycerol-3-phosphate dehydrogenase
FAD-linked L-glycerol-3-phosphate dehydrogenase
FAD-linked glycerol 3-phosphate dehydrogenase
NAD+-independent glycerol phosphate dehydrogenase
flavin-linked glycerol-3-phosphate dehydrogenase
flavoprotein-linked L-glycerol 3-phosphate dehydrogenase
glycerol 3-phosphate cytochrome c reductase [ambiguous]
glycerol phosphate dehydrogenase
glycerol phosphate dehydrogenase (FAD)
glycerol phosphate dehydrogenase (acceptor)
glycerol-3-phosphate dehydrogenase (flavin-linked)
glycerophosphate dehydrogenase
pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase
sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase
anaerobic glycerol-3-phosphate dehydrogenase
glycerol-3-phosphate CoQ reductase
glycerol-3-phosphate:CoQ reductase
mitochondrial glycerol phosphate dehydrogenase
sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
Systematic name:
sn-glycerol-3-phosphate:quinone oxidoreductase




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, 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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00753
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004368 , GO:0052590 , GO:0052591
CAS Registry Number: 9001-49-4
UniProtKB/Swiss-Prot: (120) [show] [UniProt]


  1. Ringler, R.L.
    Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain.
    J. Biol. Chem. 236: 1192-1198 (1961). [PMID: 13741763]
  2. Schryvers, A., Lohmeier, E. and Weiner, J.H.
    Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli.
    J. Biol. Chem. 253: 783-788 (1978). [PMID: 340460]
  3. MacDonald, M.J. and Brown, L.J.
    Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied.
    Arch. Biochem. Biophys. 326: 79-84 (1996). [PMID: 8579375]
  4. Rauchová, H., Fato, R., Drahota, Z. and Lenaz, G.
    Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria.
    Arch. Biochem. Biophys. 344: 235-241 (1997). [PMID: 9244403]
  5. Shen, W., Wei, Y., Dauk, M., Zheng, Z. and Zou, J.
    Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants.
    FEBS Lett. 536: 92-96 (2003). [PMID: 12586344]
  6. Walz, A.C., Demel, R.A., de Kruijff,B. and Mutzel, R.
    Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix.
    Biochem. J. 365: 471-479 (2002). [PMID: 11955283]
  7. Ansell, R., Granath, K., Hohmann, S., Thevelein, J.M. and Adler, L.
    The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation.
    EMBO J. 16: 2179-2187 (1997). [PMID: 9171333]
  8. Larsson, C., Påhlman, I.L., Ansell, R., Rigoulet, M., Adler, L. and Gustafsson, L.
    The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae.
    Yeast 14: 347-357 (1998). [PMID: 9559543]

[EC created 1961 as EC, transferred 1965 to EC, transferred 2009 to EC]