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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)
Alternate name: GDP-D-mannose dehydratase. This enzyme converts GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, the first of three steps for the conversion of GDP-mannose to GDP-fucose in animals, plants, and bacteria. In bacteria, GDP-L-fucose acts as a precursor of surface antigens such as the extracellular polysaccharide colanic acid of E. coli. Excluded from this model are members of the clade that score poorly because of highly dervied (phylogenetically long-branch) sequences, e.g. Aneurinibacillus thermoaerophilus Gmd, described as a bifunctional GDP-mannose 4,6-dehydratase/GDP-6-deoxy-D-lyxo-4-hexulose reductase (PUBMED:11096116).
GDP-mannose 4,6-dehydratase catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway
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