FAD-dependent glycerol-3-phosphate dehydrogenase (G3PDH; EC:18.104.22.168) 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:22.214.171.124) [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:0006072 glycerol-3-phosphate metabolic process
GO:0055114 oxidation-reduction process
GO:0004368 glycerol-3-phosphate dehydrogenase (quinone) activity
GO:0009331 glycerol-3-phosphate dehydrogenase complex