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NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
This is the C-terminal domain of NAD-dependent glycerol-3-phosphate dehydrogenase (GPD) from bacteria and archaea. GPD catalyses the reversible reduction of dihydroxyacetone phosphate to glycerol-3-phosphate. (from Pfam)
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus
NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyses the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the C-terminal substrate-binding domain [2]. [1]. 12032156. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. Pahlman IL, Larsson C, Averet N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M;. J Biol Chem 2002;277:27991-27995. [2]. 10801498. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Suresh S, Turley S, Opperdoes FR, Michels PA, Hol WG;. Structure Fold Des 2000;8:541-552. (from Pfam)
NAD(P)-binding domain-containing protein
2-dehydropantoate 2-reductase N-terminal domain-containing protein
This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalysed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyses the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway [2]. ApbA and PanE are allelic [2]. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway [1]. [1]. 9488683. ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway. Frodyma ME, Downs D;. J Biol Chem 1998;273:5572-5576. [2]. 9721324. The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium. Frodyma ME, Downs D;. J Bacteriol 1998;180:4757-4759. (from Pfam)
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus
NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyses the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain [2]. [1]. 12032156. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. Pahlman IL, Larsson C, Averet N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M;. J Biol Chem 2002;277:27991-27995. [2]. 10801498. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Suresh S, Turley S, Opperdoes FR, Michels PA, Hol WG;. Structure Fold Des 2000;8:541-552. (from Pfam)
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of glycerone phosphate and sn-glycerol-3-phosphate
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