PMID:10673432

Citation	Somoza, JR, Menon, S, Schmidt, H, Joseph-McCarthy, D, Dessen, A, Stahl, ML, Somers, WS and Sullivan, FX (2000) Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose. Structure 8:123-35
Abstract	GDP-mannose 4,6 dehydratase (GMD) catalyzes the conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose. This is the first and regulatory step in the de novo biosynthesis of GDP-(L)-fucose. Fucose forms part of a number of glycoconjugates, including the ABO blood groups and the selectin ligand sialyl Lewis X. Defects in GDP-fucose metabolism have been linked to leukocyte adhesion deficiency type II (LADII).
Links	PubMed
Keywords	Amino Acid Sequence; Base Sequence; Catalysis; Catalytic Domain; DNA Primers; Escherichia coli/enzymology; Guanosine Diphosphate Fucose/metabolism; Hydro-Lyases/antagonists & inhibitors; Hydro-Lyases/chemistry; Hydro-Lyases/metabolism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP/metabolism; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Sequence Homology, Amino Acid
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