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Literature summary extracted from

  • Berrisford, J.M.; Akerboom, J.; Brouns, S.; Sedelnikova, S.E.; Turnbull, A.P.; van der Oost, J.; Salmon, L.; Hardre, R.; Murray, I.A.; Blackburn, G.M.; Rice, D.W.; Baker, P.J.
    The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose isomerase provide insights into substrate binding and catalysis (2004), J. Mol. Biol., 343, 649-657.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.9 native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+ Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.9 5-phospho-D-arabinonate
-
Pyrococcus furiosus
5.3.1.9 EDTA complete inhibition Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.9 Mn2+
-
Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.9 Pyrococcus furiosus P83194
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.1.9 alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate mechanism is based on an enediol intermediate Pyrococcus furiosus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
5.3.1.9 activity of EDTA-inhibited enzyme is completely restored by addition of manganese Pyrococcus furiosus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.9 7.7
-
50°C, pH 7.0 Pyrococcus furiosus
5.3.1.9 12
-
70°C, pH 7.0 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.9 D-fructose 6-phosphate
-
Pyrococcus furiosus D-glucose 6-phosphate
-
r
5.3.1.9 D-glucose 6-phosphate
-
Pyrococcus furiosus D-fructose 6-phosphate
-
r