Literature summary for 2.7.7.12 extracted from

Wedekind, J.E.; Frey, P.A.; Rayment, I.
The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer (1996), Biochemistry, 35, 11560-11569.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09148	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose	Gln168 engages hydrogen bonding with the phosphoryl oxygen of the UMP moiety in the covalently formed reaction intermediate UMP-enzyme, UMP is bound to His166	Escherichia coli	a
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose	double-displacement mechanism	Escherichia coli	a
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose	formation of a stable nucleotidylated histidine intermediate	Escherichia coli	a
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose	mechanism model	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-glucose + alpha-D-galactose 1-phosphate	-	Escherichia coli	alpha-D-glucose 1-phosphate + UDP-galactose	-	r

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Release 2023.1 (January 2023)