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Literature summary for 3.5.99.6 extracted from

  • Lucumi-Moreno, A.; Calcagno, M.L.
    On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase (2005), Arch. Biochem. Biophys., 442, 41-48.
    View publication on PubMed
Search for more literature for 3.5.99.6

Protein Variants

Protein Variants Comment Organism
K208E entirely inactive in absence of allosteric activator N-acetylglucose-6-phosphate Escherichia coli
K208V homotropic cooperativity, Hill-coefficient 1.7, 2fold increase in dissociation constant for allosteric activator N-acetylglucose-6-phosphate compared to wild-type Escherichia coli
R172A inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant Escherichia coli
R172A/K208E inactive in absence of allosteric activator N-acetylglucose-6-phosphate, at high activator levels, cooperativity diminishes and substrate inhibition becomes significant Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
 D-glucosamine 6-phosphate mutant R172A/K208E, Michaelis-Hill equation Escherichia coli
0.55
-
 D-glucosamine 6-phosphate wild-type, Michaelis-Hill equation Escherichia coli
0.61
-
 D-glucosamine 6-phosphate mutant K208E, Michaelis-Hill equation Escherichia coli
0.69
-
 D-glucosamine 6-phosphate mutant K208V, Michaelis-Hill equation Escherichia coli
1.67
-
 D-glucosamine 6-phosphate mutant R172A, Michaelis-Hill equation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A759
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 residue R172 has a specific role in binding the substrate to the enzyme in the T state Escherichia coli
a

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
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.044
-
 D-glucosamine 6-phosphate mutant K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate Escherichia coli
6.1
-
 D-glucosamine 6-phosphate mutant R172A/K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate Escherichia coli
7.8
-
 D-glucosamine 6-phosphate mutant K208V, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate Escherichia coli
11.8
-
 D-glucosamine 6-phosphate mutant R172A, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate Escherichia coli
160
-
 D-glucosamine 6-phosphate wild-type, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate Escherichia coli