Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase.
Copyright policy )Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase.
UDP-6-deoxygalactose inhibits the UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli in a competitive manner with respect to the substrate UDP-galactose, giving K(i) 1.3x10(-3)m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained. Possible causes of this behaviour are discussed.
Kinetics, Glucose, Magnetic Resonance Spectroscopy, Time Factors, Escherichia coli, Galactose, Chromatography, Thin Layer, Carbohydrate Epimerases, Deuterium, Uridine Diphosphate Sugars, Binding, Competitive
Kinetics, Glucose, Magnetic Resonance Spectroscopy, Time Factors, Escherichia coli, Galactose, Chromatography, Thin Layer, Carbohydrate Epimerases, Deuterium, Uridine Diphosphate Sugars, Binding, Competitive
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