FAD-dependent glycerol-3-phosphate dehydrogenase (IPR000447)

Short name: G3P_DH_FAD-dep

Overlapping homologous superfamilies

Family relationships


FAD-dependent glycerol-3-phosphate dehydrogenase (G3PDH; EC: catalyses the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate: sn-glycerol-3-phosphate + a quinone = glycerone phosphate + a quinol Insulin exposure often stimulates G3PDH activity [PMID: 7857262, PMID: 8954787], and thus is key to reducing the effects of the disease diabetes. In obese people, where insulin resistance has been demonstrated, the amount of G3PDH has been shown to be correspondingly lower than that in normal weight people [PMID: 7857262]. In bacteria [PMID: 1987111] it is associated with the utilization of glycerol coupled to respiration. In Escherichia coli and Haemophilus influenzae, two isozymes are known: one expressed under anaerobic conditions (gene glpA) and one in aerobic conditions (gene glpD). In eukaryotes, a mitochondrial form of GPD participates in the glycerol phosphate shuttle in conjunction with an NAD-dependent cytoplasmic GPD (EC: [PMID: 8256521, PMID: 8182039]. This mechanism is responsible for the preservation of a redox balance [PMID: 8760382, PMID: 9559543]. In this environment, the enzyme has been recorded to increase activity in the presence of calcium [PMID: 8579375]. These enzymes are proteins of about 60 to 70 Kd which contain a probable FAD-binding domain in their N-terminal extremity. The mammalian enzyme differs from the bacterial or yeast proteins by having an EF-hand calcium-binding region (see PDOC00018) in its C-terminal extremity.

GO terms

Biological Process

GO:0006072 glycerol-3-phosphate metabolic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0004368 glycerol-3-phosphate dehydrogenase (quinone) activity

Cellular Component

GO:0009331 glycerol-3-phosphate dehydrogenase complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns