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Literature summary for 3.5.99.6 extracted from

  • Bustos-Jaimes, I.; Calcagno, M.L.
    Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli (2001), Arch. Biochem. Biophys., 394, 156-160.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
N-acetylglucosamine 6-phosphate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 thermodynamic study, the allosteric behavior of enzyme can be described by the Monod-Wyman-Changeux model Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-fructose 6-phosphate + NH3
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
effect of temperature on homotropic co-operativity in the enzyme Escherichia coli