glycerol-3-phosphate dehydrogenase (NAD+)

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For detailed information about glycerol-3-phosphate dehydrogenase (NAD+), go to the full flat file.

Word Map on EC


sn-glycerol 3-phosphate
glycerone phosphate
reduced acceptor


(NAD+)-dependent G3pdh, (NAD+)-dependent glycerol-3-phosphate dehydrogenase, alpha glycerophosphate dehydrogenase, alpha-glycerol phosphate dehydrogenase (NAD), alpha-glycerophosphate dehydrogenase (NAD), Cagpd1, Cagpd1p, Cagpd2, Cagpd2p, cG3PDH, CgGPD, cGPdH, cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase, cytosolic GPDH, dehydrogenase, glycerol phosphate, DhGPD1, G-3-P dehydrogenase, G3P dehydrogenase, G3PD, G3PD1, G3PD2, G3PD3, G3PDH, GDM, GDP2, GLPD, GLY1, 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, Gpd1p, gpd2p, GPDH, GPDH-1, GPDH-2, GPDH1, GPDH2, GPDH3, GPDH: NAD+ 2 oxidoreductase, 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 G3P dehydrogenase, 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, NADP+-dependent glycerol 3-phosphate dehydrogenase, SFD1, SFD1/GLY1


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


Engineering on EC - glycerol-3-phosphate dehydrogenase (NAD+)

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site-direted mutagenesis, the mutation results in a 7.7 kcal/mol decrease in the intrinsic phosphodianion binding energy, which is larger than the 5.6 kcal/mol effect of the mutation on the stability of the transition state for reduction of DHAP. A 2.2 kcal/mol stabilization of the transition state for unactivated hydride transfer to the truncated substrate glycolaldehyde, and a change in the effect of phosphite dianion on GPDH-catalyzed reduction of glycolaldehyde, from strongly activating to inhibiting. The N270A mutation breaks the network of hydrogen bonding side chains, Asn270, Thr264, Asn205, Lys204, Asp260, and Lys120, which connect the dianion activation and catalytic sites of GPDH. The disruption dramatically alters the performance of GPDH at these sites. The mutant enzyme shows highly decreased activity compared to the wild-type with glycerone phosphate,but 40fold higher activity with glycolaldehyde compared to the wild-type. There is no significant rescue of the activity of the N270A mutant with glycerone phosphate by 60 mM formamide; the mutant shows a strong decrease in catalytic efficiency compared to the wild type enzyme
site-direted mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type. The N270A mutation at R269A hlGPDH results in the loss of the intrinsic side chain-dianion interaction; the mutant shows a strong decrease in catalytic efficiency compared to the wild type enzyme
anaerobic growth, growth rate and glycerol production similar to wild-type
anaerobic growth, growth rate and glycerol production similar to wild-type
50% decrease in anaerobic glycerol production
no growth under anaerobic or aerobic conditions
additional information