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Literature summary for 3.5.99.6 extracted from

  • Montero-Moran, G.M.; Lara-Gonzalez, S.; Alvarez-Anorve, L.I.; Plumbridge, J.A.; Calcagno, M.L.
    On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase (2001), Biochemistry, 40, 10187-10196.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D141N the mutation modifies the kcat versus pH profile of the enzyme Escherichia coli
D141N/E148Q mutation modifies the kcat versus pH profile of the enzyme Escherichia coli
E148Q the mutation modifies the kcat versus pH profile of the enzyme Escherichia coli
H143Q drastically impairs the activity of the enzyme in the forward but not in the backward direction of the reaction Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2,5-anhydro mannitol 6-phosphate
-
Escherichia coli
2-deoxy-2-amino-D-glucitol 6-phosphate
-
Escherichia coli
D-fructose 6-phosphate
-
Escherichia coli
D-fructose oxime 6-phosphate
-
Escherichia coli
diethyl dicarbonate complete inactivation, 2-deoxy-2-amino-D-glucitol 6-phosphate protects Escherichia coli
additional information not: alpha and beta O-methyl glycoside of D-fructose 6-phosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information comparison of KM of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators 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 His143 has many functional roles in the active site of enzyme 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
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information comparison of kcat of mutant H143Q and wild-type enzyme for the forward and backward reactions in absence and presence of activators Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
pH dependence of the reactivity of the active site histidine to diethyl dicarbonate Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.002
-
2-deoxy-2-amino-D-glucitol 6-phosphate pH 7.8, 25°C Escherichia coli
1.3
-
D-fructose oxime 6-phosphate pH 7.7, 30°C Escherichia coli
13.4
-
2,5-anhydro mannitol 6-phosphate pH 7.7, 30°C Escherichia coli