Literature summary for 1.1.1.22 extracted from

Sennett, N.C.; Kadirvelraj, R.; Wood, Z.A.
Cofactor binding triggers a molecular switch to allosterically activate human UDP-alpha-D-glucose 6-dehydrogenase (2012), Biochemistry, 51, 9364-9374.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant K94E, to 2.08 A resolution. Cofactor binding triggers the formation of the 32 symmetry hexamer, but substrate UDP-alpha-D-glucose is needed for the stability of the complex. Loop88-110 is the cofactor-responsive allosteric switch that drives hexamer formation, loop88-110 directly links cofactor binding to the stability of the hexamer-building interface. In the interface, loop88-110 packs against the Thr131-loop/alpha6 helix, the allosteric switch that responds to the feedback inhibitor UDP-alpha-D-xylose	Homo sapiens

Crystallization (Comment)

Organism

mutant K94E, to 2.08 A resolution. Cofactor binding triggers the formation of the 32 symmetry hexamer, but substrate UDP-alpha-D-glucose is needed for the stability of the complex. Loop88-110 is the cofactor-responsive allosteric switch that drives hexamer formation, loop88-110 directly links cofactor binding to the stability of the hexamer-building interface. In the interface, loop88-110 packs against the Thr131-loop/alpha6 helix, the allosteric switch that responds to the feedback inhibitor UDP-alpha-D-xylose

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
K94E	mutation in the hexamer-building interface, generates a stable enzyme dimer. 160fold decrease in kcat value	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.025	-	UDP-alpha-D-glucose	wild-type, pH 8.7, 25°C	Homo sapiens
0.384	-	NAD+	wild-type, pH 8.7, 25°C	Homo sapiens
2.21	-	UDP-alpha-D-glucose	mutant K94E, pH 8.7, 25°C	Homo sapiens
6.3	-	NAD+	mutant K94E, pH 8.7, 25°C	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60701	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-alpha-D-glucose + 2 NAD+ + H2O	-	Homo sapiens	UDP-alpha-D-glucuronate + 2 NADH + 2 H+	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.02	-	NAD+	mutant K94E, pH 8.7, 25°C	Homo sapiens
0.02	-	UDP-alpha-D-glucose	mutant K94E, pH 8.7, 25°C	Homo sapiens
3.2	-	UDP-alpha-D-glucose	wild-type, pH 8.7, 25°C	Homo sapiens
4.4	-	NAD+	wild-type, pH 8.7, 25°C	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	cofactor binding triggers the formation of the 32 symmetry enzyme hexamer, which is the catalytically relevant state	Homo sapiens