Literature summary for 2.7.1.2 extracted from

Lunin, V.V.; Li, Y.; Schrag, J.D.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose (2004), J. Bacteriol., 186, 6915-6927.

Cloned(Commentary)

Cloned (Comment)	Organism
gene glk, expression of His-tagged enzyme in strain BL21(DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant selenomethionine-labeled enzyme free or in complex with D-glucose, hanging drop vapour diffusion method, 0.002 ml enzyme solution containing 6.8 mg/ml protein mixed with 0.004 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 1.7 M ammonium sulfate for the apo-enzyme or 18.5-20% PEG 6000 with 2 mM D-glucose and 2-3 mM ADP for the glucose-bound enzyme, X-ray diffraction structure determination and analysis at 2.3-2.2 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant selenomethionine-labeled enzyme free or in complex with D-glucose, hanging drop vapour diffusion method, 0.002 ml enzyme solution containing 6.8 mg/ml protein mixed with 0.004 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 1.7 M ammonium sulfate for the apo-enzyme or 18.5-20% PEG 6000 with 2 mM D-glucose and 2-3 mM ADP for the glucose-bound enzyme, X-ray diffraction structure determination and analysis at 2.3-2.2 A resolution

Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + D-glucose	Escherichia coli	-	ADP + D-glucose 6-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6V9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + D-glucose = ADP + D-glucose 6-phosphate	catalytic mechanism, substrate D-glucose interacts with Asn99, Asp100, Glu157, His160, and Glu187	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + D-glucose	-	Escherichia coli	ADP + D-glucose 6-phosphate	-	?
ATP + D-glucose	specific for D-glucose, substrate binding site structure	Escherichia coli	ADP + D-glucose 6-phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimer, crystal structure determination	Escherichia coli
More	the active site is located in a deep cleft between the 2 domains of each subunit, monomer and dimer structures, overview	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	dependent on, binding site structure	Escherichia coli