Literature summary for 5.3.1.9 extracted from

Swan, M.K.; Solomons, J.T.; Beeson, C.C.; Hansen, T.; Schoenheit, P.; Davies, C.
Structural evidence for a hydride transfer mechanism of catalysis in phosphoglucose isomerase from Pyrococcus furiosus (2003), J. Biol. Chem., 278, 47261-47268.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	P83194	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate	in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates	Pyrococcus furiosus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose 6-phosphate	in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms	Pyrococcus furiosus	D-fructose 6-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
Phosphoglucose isomerase	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)