Protein Family Models

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)

Date:

2024-08-14

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)

Date:

2024-10-16

Acetohydroxy acid isomeroreductase catalyses the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, Pfam:PF01450. [1]. 9218783. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E;. EMBO J 1997;16:3405-3415. [2]. 16322583. The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG;. Protein Sci. 2005;14:3089-3100. [3]. 19362563. Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures. Leung EW, Guddat LW;. J Mol Biol. 2009;389:167-182. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)

Date:

2024-08-14

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)

Date:

2024-10-16

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)

Date:

2024-10-16