PMID:9817848
| Citation |
Rizzi, M, Tonetti, M, Vigevani, P, Sturla, L, Bisso, A, Flora, AD, Bordo, D and Bolognesi, M (1998) 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. Structure 6:1453-65 |
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| Abstract |
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/reductase (GMER). Neither of the catalytic mechanisms nor the three-dimensional structures of the two enzymes has been elucidated yet. The severe leukocyte adhesion deficiency (LAD) type II genetic syndrome is known to result from deficiencies in this de novo pathway. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Carbohydrate Epimerases/chemistry; Carbohydrate Epimerases/metabolism; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Escherichia coli Proteins; Guanosine Diphosphate Fucose/biosynthesis; Humans; Ketone Oxidoreductases; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; NADP/metabolism; Protein Conformation; Protein Folding; Sequence Homology, Amino Acid; Sugar Alcohol Dehydrogenases/chemistry; Sugar Alcohol Dehydrogenases/metabolism |
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