Literature summary for 5.3.1.8 extracted from

May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.
Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa (1994), J. Biol. Chem., 269, 4872-4877.

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-Mannose 6-phosphate	-	Pseudomonas aeruginosa	D-Fructose 6-phosphate	-	?

Subunits

Subunits	Comment	Organism
More	bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is composed of two independent enzymatic domains. The carboxyl terminus is critical for mannose-6-phosphate isomerase	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)