| Description | FAD-dependent glycerol-3-phosphate dehydrogenase (G3PDH; ) catalyses the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate: sn-glycerol-3-phosphate + a quinone = glycerone phosphate + a quinolInsulin exposure often stimulates G3PDH activity [ , ], 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 []. In bacteria [] it is associated with the utilisation 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 () [ , ]. This mechanism is responsible for the preservation of a redox balance [, ]. In this environment, the enzyme has been recorded to increase activity in the presence of calcium []. 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 ) in its C-terminal extremity. | Name | FAD-dependent glycerol-3-phosphate dehydrogenase |
| Short Name | G3P_DH_FAD-dep | Type | Family |
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