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Literature summary for 3.5.99.6 extracted from

  • Rudino-Pinera, E.; Morales-Arrieta, S.; Rojas-Trejo, S.P.; Horjales, E.
    Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase (2002), Acta Crystallogr. Sect. D, 58, 10-20.
    View publication on PubMed

Activating Compound

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

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure of five complexes of the enzyme in R and T state is described and their kinetic and allosteric implication analysed, the ligand-free enzyme, T-conformer, undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A759
-
-

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
-
?
additional information the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route Escherichia coli ?
-
?