Literature summary for 2.7.7.12 extracted from

Ruzicka, F.J.; Wedekind, J.E.; Kim, J.; Rayment, I.; Frey, P.A.
Galactose-1-phosphate uridylyltransferase from Escherichia coli, a zinc and iron metalloenzyme (1995), Biochemistry, 34, 5610-5617.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in strain BL21	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
1,10-phenanthroline	inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions, UDP-glucose protects, but alpha-D-glucose 1-phosphate does not	Escherichia coli
2,2'-bipyridyl	inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions	Escherichia coli
8-hydroxyquinoline	inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions	Escherichia coli
8-Hydroxyquinoline sulfonate	inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	required	Escherichia coli
Fe2+	0.7 mol per mol of subunit	Escherichia coli
additional information	enzyme contains no Ca, Cd, Cu, Mo, Ni, Co, Mn, As, Pb, or Se	Escherichia coli
Zn2+	required	Escherichia coli
Zn2+	1.2 mol tightly bound per mol of subunit	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from overexpressing strain BL21(DE3)	Escherichia coli
to homogeneity	Escherichia coli

Renatured (Commentary)

Renatured (Comment)	Organism
enzyme reconstitution with different metal ions after denaturation with urea to eliminate the natively bound metal ions	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
170	190	purified recombinant enzyme	Escherichia coli

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)