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- W2090706502 abstract "The structure of the NAD-dependent oxidoreductase UDP-galactose-4′-epimerase from Trypanosoma brucei in complex with cofactor and the substrate analogue UDP-4-deoxy-4-fluoro-α-d-galactose has been determined using diffraction data to 2.7 Å resolution. Despite the high level of sequence and structure conservation between the trypanosomatid enzyme and those from humans, yeast and bacteria, the binding of the 4-fluoro-α-d-galactose moiety is distinct from previously reported structures. Of particular note is the observation that when bound to the T. brucei enzyme, the galactose moiety of this fluoro-derivative is rotated approximately 180° with respect to the orientation of the hexose component of UDP-glucose when in complex with the human enzyme. The architecture of the catalytic centre is designed to effectively bind different orientations of the hexose, a finding that is consistent with a mechanism that requires the sugar to maintain a degree of flexibility within the active site." @default.
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- W2090706502 date "2006-08-11" @default.
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- W2090706502 title "<i>Trypanosoma brucei</i>UDP-galactose-4′-epimerase in ternary complex with NAD<sup>+</sup>and the substrate analogue UDP-4-deoxy-4-fluoro-α-<scp>D</scp>-galactose" @default.
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- W2090706502 doi "https://doi.org/10.1107/s1744309106028740" @default.
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