PMID:11916143

Citation	Todorova, R (2001) Isomerase activity of the C-terminal fructose-6-phosphate binding domain of glucosamine-6-phosphate synthase from Escherichia coli. J. Enzym. Inhib. 16:373-80
Abstract	The isomerase activity of the C-terminal fructose-6P binding domain (residues 241-608) of glucosamine-6-phosphate synthase from Escherichia coli has been studied. The equilibrium constant of the C-terminal domain k(eq) ([glucose-6P]/[fructose-6-P]) = 5.0. A non-competitive product inhibition of the isomerase activity by the reaction product glucose-6-P has been detected. The existence of more than one binding and reaction sites for the substrate fructose-6P on the molecule of glucosamine-6-phosphate synthase can be expected. The fructose-6P binding domain possibly includes a regulatory site, different from the catalytic center of the enzyme.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Escherichia coli/enzymology; Fructosephosphates; Glucose-6-Phosphate/pharmacology; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/antagonists & inhibitors; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/chemistry; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/metabolism; Isomerases/antagonists & inhibitors; Isomerases/chemistry; Isomerases/metabolism; Isomerism; Kinetics; Protein Structure, Tertiary
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