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Literature summary for 3.5.99.6 extracted from

  • Bustos-Jaimes, I.; Sosa-Peinado, A.; Rudino-Pinera, E.; Horjales, E.; Calcagno, M.L.
    On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase (2002), J. Mol. Biol., 319, 183-189.
    View publication on PubMed
Search for more literature for 3.5.99.6

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystallographic structure of F174A is determinated Escherichia coli

Protein Variants

Protein Variants Comment Organism
F174A the mutation effectively weakens the interaction between the active-site lid and the rest of the enzyme molecule, the mutant is essentially inactive in the absence of its allosteric activator Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-deoxy-2-amino-D-glucitol 6-phosphate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.55
-
 D-glucosamine 6-phosphate pH 7.5, 30°C, wild-type enzyme, in presence of N-acetylglucosamine 6-phosphate Escherichia coli
3.43
-
 D-glucosamine 6-phosphate pH 7.5, 30°C, mutant F174A, in presence of N-acetylglucosamine 6-phosphate Escherichia coli

Organism

Organism UniProt Comment Textmining
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
-
 ?