PMID:11700065

Citation	Teplyakov, A, Obmolova, G, Badet, B and Badet-Denisot, MA (2001) Channeling of ammonia in glucosamine-6-phosphate synthase. J. Mol. Biol. 313:1093-102
Abstract	Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.
Links	PubMed Online version:10.1006/jmbi.2001.5094
Keywords	Ammonia/metabolism; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Glutaminase/chemistry; Glutaminase/metabolism; Glutamine/metabolism; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/chemistry; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/metabolism; Isomerases/chemistry; Isomerases/metabolism; Models, Molecular; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Nitrogen/metabolism; Protein Structure, Quaternary; Protein Structure, Tertiary; Solvents; Structure-Activity Relationship
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