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NAD-binding protein
3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1]. [1]. 16126223. Crystal structure of novel NADP-dependent 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8. Lokanath NK, Ohshima N, Takio K, Shiromizu I, Kuroishi C, Okazaki N, Kuramitsu S, Yokoyama S, Miyano M, Kunishima N;. J Mol Biol. 2005;352:905-917. (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
NAD(P)-dependent oxidoreductase such as sulfolactaldehyde 3-reductase, which reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS)
sulfolactaldehyde 3-reductase
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