Literature summary for 5.3.1.9 extracted from

Lee, J.H.; Chang, K.Z.; Patel, V.; Jeffery, C.J.
Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate (2001), Biochemistry, 40, 7799-7805.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution	Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Oryctolagus cuniculus	the enzyme plays important roles in glycolysis and gluconeogenesis	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	Q9N1E2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose 6-phosphate	multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2	Oryctolagus cuniculus	D-fructose 6-phosphate	-	r
additional information	the enzyme plays important roles in glycolysis and gluconeogenesis	Oryctolagus cuniculus	?	-	?

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Release 2023.1 (January 2023)