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Literature summary extracted from

  • Bustos-Jaimes, I.; Ramirez-Costa, M.; De Anda-Aguilar, L.; Hinojosa-Ocana, P.; Calcagno, M.L.
    Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase (2005), Biochemistry, 44, 1127-1135.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.99.6 W15Y mutant containing a single Trp residue at W224 Escherichia coli
3.5.99.6 W15Y/F174W/W224Y mutant containing a single, new Trp-residue at F174W Escherichia coli
3.5.99.6 W15Y/W224Y mutant without Trp residues Escherichia coli
3.5.99.6 W15Y/W224Y/Y254W mutant containing a single, new Trp-residue at Y254W Escherichia coli
3.5.99.6 W224Y mutant containing a single Trp residue at W15 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.99.6 2-deoxy-2-amino-D-glucitol 6-phosphate
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.99.6 0.26
-
D-glucosamine 6-phosphate mutant W15Y/W224Y/Y254W, pH 7.5, S0.5-value 0.5 mM Escherichia coli
3.5.99.6 0.49
-
D-glucosamine 6-phosphate mutant W15Y/F174W/W224Y, pH 7.5, S0.5-value 3.4 mM Escherichia coli
3.5.99.6 0.5
-
D-glucosamine 6-phosphate mutant W224Y, pH 7.5, S0.5-value 4.8 mM Escherichia coli
3.5.99.6 0.55
-
D-glucosamine 6-phosphate wild-type, pH 7.5, S0.5-value 5.5 mM Escherichia coli
3.5.99.6 0.62
-
D-glucosamine 6-phosphate mutant W15Y, pH 7.5, S0.5-value 5.8 mM Escherichia coli
3.5.99.6 0.65
-
D-glucosamine 6-phosphate mutant W15Y/W224Y, pH 7.5, S0.5-value 5.0 mM Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.99.6 Escherichia coli P0A759
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 enzyme-activator and enzyme-inhibitor complex have strucutral differences that also differ from ternary complex enzyme-activator-inhibitor. The occupation of the active site generates structural perturbations which extend to the other subunits, resulting in predominance of the R over the T forms in the population of deaminase hexamers Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.6 D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-fructose 6-phosphate + NH3
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.99.6 26.7
-
D-glucosamine 6-phosphate mutant W15Y/W224Y/Y254W, pH 7.5 Escherichia coli
3.5.99.6 80
-
D-glucosamine 6-phosphate mutant W15Y/F174W/W224Y, pH 7.5 Escherichia coli
3.5.99.6 134
-
D-glucosamine 6-phosphate mutant W15Y, pH 7.5 Escherichia coli
3.5.99.6 138
-
D-glucosamine 6-phosphate mutant W224Y, pH 7.5 Escherichia coli
3.5.99.6 144
-
D-glucosamine 6-phosphate mutant W15Y/W224Y, pH 7.5 Escherichia coli
3.5.99.6 158
-
D-glucosamine 6-phosphate wild-type, pH 7.5 Escherichia coli