Literature summary for 5.1.3.2 extracted from

Wei, Y.; Lin, J.; Frey, P.A.
13C NMR analysis of electrostatic interactions between NAD+ and active site residues of UDP-galactose 4-epimerase: implications for the activation induced by uridine nucleotides (2001), Biochemistry, 40, 11279-11287.

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Protein Variants

Protein Variants	Comment	Organism
K153M	mutation results in a 13C chemical shift of 150.8 ppm, which is 0.9 ppm downfield from that of wild-type and 1.8 ppm upfield from that of Y149F epimerase	Escherichia coli
S124A/Y149F	mutation causes a 13C downfield perturbation of 2.8 ppm to 152.7 ppm	Escherichia coli
Y149F	mutation results in a 13C downfield perturbation of 2.7 ppm to 152.6 ppm	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09147	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-galactose	-	Escherichia coli	UDP-glucose	-	r

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	coenzyme is tightly bound at the active site. NAD+ functions as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating their dehydrogenation to the common intermediate UDP-4-ketohexopyranoside. NAD+ activation induced by uridine nucleotides is brought about by a conformational change of epimerase that repositions Tyr149 at an increased distance from nicotinamide N1 of NAD+ while maintaining the electrostatic repulsion between Lys153 and nicotinamide N1 of NAD+	Escherichia coli

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Release 2023.1 (January 2023)