GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily.

@article{Rizzi1998GDP4keto6deoxyDmannoseEF,
  title={GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily.},
  author={Menico Rizzi and Michela G. Tonetti and P Vigevani and Laura Sturla and Angela Bisso and Antonio de Flora and D. Bordo and Martino Bolognesi},
  journal={Structure},
  year={1998},
  volume={6 11},
  pages={1453-65}
}
BACKGROUND The process of guanosine 5'-diphosphate L-fucose (GDP-L-fucose) biosynthesis is conserved throughout evolution from prokaryotes to man. In animals, GDP-L-fucose is the substrate of fucosyltransferases that participate in the biosynthesis and remodeling of glycoconjugates, including ABH blood group and Lewis-system antigens. The 'de novo' pathway of GDP-L-fucose biosynthesis from GDP-D-mannose involves a GDP-D-mannose 4,6 dehydratase (GMD) and a GDP-4-keto-6-deoxy-D-mannose epimerase… CONTINUE READING

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The crystal structure of human GDP-L-fucose synthase.

Acta biochimica et biophysica Sinica • 2013

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