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Selected Publication:

Blankenfeldt, W; Kerr, ID; Giraud, MF; McMiken, HJ; Leonard, G; Whitfield, C; Messner, P; Graninger, M; Naismith, JH.
(2002): Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerization mode.
Structure. 2002; 10(6):773-786

dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmID) catalyzes the final step in the conversion of dTDP-D-glucose to dTDP-L-rhamnose in an NAD(P)H- and Mg2+-dependent reaction. L-rhamnose biosynthesis is an antibacterial target. The structure of RmID from Salmonella enterica serovar Typhimurium has been determined, and complexes with NADH, NADPH, and dTDP-L-rhamnose are reported. RmID differs from other short chain dehydrogenases in that it has a novel dimer interface that contains Mg2+. Enzyme catalysis involves hydride transfer from the nicotinamide ring of the cofactor to the C4'-carbonyl group of the substrate. The substrate is activated through protonation by a conserved tyrosine. NAD(P)H is bound in a solvent-exposed cleft, allowing facile replacement. We suggest a novel role for the conserved serine/threonine residue of the catalytic triad of SDR enzymes.
Authors BOKU Wien:
Messner Paul
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Bacterial Proteins - chemistry
Binding Sites -
Dimerization -
Magnesium - metabolism
Mutagenesis, Site-Directed -
NAD - metabolism
NADP - metabolism
Protein Structure, Tertiary -
Salmonella enterica - enzymology
Sugar Alcohol Dehydrogenases - chemistry

Find related publications in this database (Keywords)
drug design
Salmonella enterica serovar Typhimurium

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