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GDP-mannose 4,6-dehydratase
sugar nucleotide-binding protein
L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide [1,2]. [1]. 12057193. Variation on a Theme of SDR. dTDP-6-Deoxy-L- lyxo-4-Hexulose Reductase (RmlD) Shows a New Mg(2+)-Dependent Dimerization Mode. Blankenfeldt W, Kerr ID, Giraud MF, McMiken HJ, Leonard G, Whitfield C, Messner P, Graninger M, Naismith JH;. Structure (Camb) 2002;10:773-786. [2]. 10802738. RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase. Giraud MF, Leonard GA, Field RA, Berlind C, Naismith JH;. Nat Struct Biol 2000;7:398-402. (from Pfam)
NAD-dependent epimerase/dehydratase family protein
This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. [1]. 9174344. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM;. Biochemistry 1997;36:6294-6304. (from Pfam)
GDP-L-fucose synthase family protein
GDP-L-fucose synthase family protein such as GDP-L-fucose synthase that catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction; belongs to the extended (e) SDR (short-chain dehydrogenase/reductase) family; in addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids
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