Literature summary extracted from

Berrisford, J.M.; Akerboom, J.; Turnbull, A.P.; de Geus, D.; Sedelnikova, S.E.; Staton, I.; McLeod, C.W.; Verhees, C.H.; Van der Oost, J.; Rice, D.W.; Baker, P.J.
Crystal structure of Pyrococcus furiosus phosphoglucose isomerase: implications for substrate binding and catalysis (2003), J. Biol. Chem., 278, 33290-33297.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
5.3.1.9	structure is determined by X-ray diffraction to 2 A resolution	Pyrococcus furiosus

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
5.3.1.9	Fe2+	bound to the enzyme. Catalytic activity is not strongly influenced either by the replacement of Fe2+ by a range of transition metals or by the presence or absence of the bound metal ion. The metal may not directly involved in catalysis but rather may be implicated in substrate recognition	Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5.3.1.9	additional information	Pyrococcus furiosus	the enzyme is part of the glycolytic pathway	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.3.1.9	Pyrococcus furiosus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.3.1.9	D-glucose 6-phosphate	-	Pyrococcus furiosus	D-fructose 6-phosphate	-	r
5.3.1.9	additional information	the enzyme is part of the glycolytic pathway	Pyrococcus furiosus	?	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
5.3.1.9	PGI	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)