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Acetohydroxy acid isomeroreductase, NADPH-binding domain
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)
NAD(P)-binding domain-containing protein
The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)
NAD(P)-dependent oxidoreductase
This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate. dehydrogenase from Lactobacillus casei, NAD+ and. 2-oxoisocaproate at 1.9 A resolution.. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)
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)
Acetohydroxy acid isomeroreductase, catalytic domain
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. [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. (from Pfam)
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