Literature summary for 2.7.7.12 extracted from

Thoden, J.B.; Ruzicka, F.J.; Frey, P.A.; Rayment, I.; Holden, H.M.
Structural analysis of the H166G site-directed mutant of galactose 1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site (1997), Biochemistry, 36, 1212-1222.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
H166G mutant enzyme/UDP-glucose or UDP-galactose complexes, X-ray diffraction structure determination and analysis	Escherichia coli
uridyl/enzyme complex, X-ray diffraction structure determination and analysis	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
H166G	-	Escherichia coli

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	active site nucleophil H166	Escherichia coli	a
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose	amino acid residues of both subunits contribute to the active site	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)