1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+)

This is an abbreviated version, for detailed information about glycerol-3-phosphate dehydrogenase (NAD+), go to the full flat file.

Reaction

sn-glycerol 3-phosphate
+
acceptor
=
glycerone phosphate
+
reduced acceptor

Synonyms

(NAD+)-dependent G3pdh, (NAD+)-dependent glycerol-3-phosphate dehydrogenase, alpha glycerophosphate dehydrogenase, alpha-glycerol phosphate dehydrogenase (NAD), alpha-glycerophosphate dehydrogenase (NAD), Cagpd1, Cagpd2, cG3PDH, CgGPD, cGPdH, cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase, dehydrogenase, glycerol phosphate, DhGPD1, G-3-P dehydrogenase, G3P dehydrogenase, G3PD, G3PDH, GDM, GDP2, GLPD, glycerol 1-phosphate dehydrogenase, glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate dehydrogenase 1, glycerol phosphate dehydrogenase (NAD), glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase 1, glycerophosphate dehydrogenase (NAD), GPD, GPD1, GPDH, GPDH-1, GPDH-2, GPDH1, GPDH2, GPDH: NAD+ 2 oxidorreductase, GPDHc1, hydroglycerophosphate dehydrogenase, L-alpha-glycerol phosphate dehydrogenase, L-alpha-glycerophosphate dehydrogenase, L-glycerol 3-phosphate dehydrogenase, L-glycerol phosphate dehydrogenase, L-glycerophosphate dehydrogenase, mGPDH, NAD+-dependent glycerol 3-phosphate dehydrogenase, NAD+-dependent glycerol-3-phosphate dehydrogenase, NAD+-GPDH, NAD-alpha-glycerophosphate dehydrogenase, NAD-dependent cG3PDH, NAD-dependent glycerol phosphate dehydrogenase, NAD-dependent glycerol-3-phosphate dehydrogenase, NAD-L-glycerol-3-phosphate dehydrogenase, NAD-linked glycerol 3-phosphate dehydrogenase, NADH-dihydroxyacetone phosphate reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)

Application

Application on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+)

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
medicine
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the hyperthyroid status leads to a significant decrease and the hypothyroid status to a significant increase of both enzyme amount and activity in both female and male animals. The euthyroid and hyperthyroid females show a higher activity and the hyperthyroid females also show a higher enzyme amount in comparison with male animals, while the hypothyroid animals show low levels in both sexes. The enzyme-dependent oxygen consumption of freshly isolated liver mitochondria from hyperthyroid animals is higher compared with euthyroid animals, and is activated bycoenzyme Q analogue idebenone, in both euthyroid and hyperthyroid rats. Determination of enzyme amount and activity can serve as an additional criterion for the evaluation of the thyroid hormone status
nutrition
synthesis