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Literature summary extracted from

  • Alvarez-Anorve, L.I.; Gaugue, I.; Link, H.; Marcos-Viquez, J.; Diaz-Jimenez, D.M.; Zonszein, S.; Bustos-Jaimes, I.; Schmitz-Afonso, I.; Calcagno, M.L.; Plumbridge, J.
    Allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase (NagB) in vivo justified by intracellular amino sugar metabolite concentrations (2016), J. Bacteriol., 198, 1610-1620 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.99.6 GlcNAc6P enzyme NagB is allosterically activated by GlcNAc6P Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.99.6 gene nagB Escherichia coli
3.5.99.6 gene nagB, recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, resulting in LAA195 (nagBBs+) Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.5.99.6 additional information construction of bacterial strains LAA199 (nagBEc+) and LAA195 (nagBBs+). The gene for the Escherichia coli allosteric NagBEc enzyme is replaced with that of the nonallosteric Bacillus subtilis homologue NagBBs. No effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB. Deletion of the nagB gene had no strong effect on the amino sugar pools Escherichia coli
3.5.99.6 additional information recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.99.6 0.85
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Escherichia coli
3.5.99.6 1.5
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O Escherichia coli
-
 D-fructose 6-phosphate + NH3
-
 ?
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O Bacillus subtilis
-
 D-fructose 6-phosphate + NH3
-
 ?
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O Bacillus subtilis 168
-
 D-fructose 6-phosphate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.99.6 Bacillus subtilis O35000
-
-
3.5.99.6 Bacillus subtilis 168 O35000
-
-
3.5.99.6 Escherichia coli P0A759
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O
-
 Escherichia coli D-fructose 6-phosphate + NH3
-
 ?
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O
-
 Bacillus subtilis D-fructose 6-phosphate + NH3
-
 ?
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O
-
 Bacillus subtilis 168 D-fructose 6-phosphate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.99.6 glucosamine-6-phosphate deaminase 1
-
 Bacillus subtilis
3.5.99.6 glucosamine-6P deaminase
-
 Escherichia coli
3.5.99.6 glucosamine-6P deaminase
-
 Bacillus subtilis
3.5.99.6 NagB
-
 Escherichia coli
3.5.99.6 NagB
-
 Bacillus subtilis
3.5.99.6 NagBBs
-
 Bacillus subtilis
3.5.99.6 NagBEc
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.99.6 37
-
 assay at Escherichia coli
3.5.99.6 37
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.99.6 110
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Bacillus subtilis
3.5.99.6 220
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.99.6 7.4
-
 assay at Escherichia coli
3.5.99.6 7.4
-
 assay at Bacillus subtilis

General Information

EC Number General Information Comment Organism
3.5.99.6 metabolism controlling the biosynthetic and degradative pathways of amino sugar metabolism is important in all organisms to avoid loss of nitrogen and energy via a futile cycle of synthesis and breakdown. The enzyme glucosamine-6P deaminase (NagB) is central to this control, and N-acetylglucosamine-6P is the key signaling molecule regulating amino sugar utilization in Escherichia coli Escherichia coli
3.5.99.6 physiological function the enzyme glucosamine-6P deaminase (NagB) is required for growth on both GlcN and GlcNAc. It is an allosteric enzyme in Escherichia coli, displaying sigmoid kinetics with respect to its substrate, GlcN6P, and is allosterically activated by GlcNAc6P. The high concentration of GlcN6P, accompanied by the small increase in GlcNAc6P, drives Escherichia coli NagB (NagBEc) into its high activity state, as observed during growth on GlcN Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.99.6 73.3
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Bacillus subtilis
3.5.99.6 258.8
-
 alpha-D-glucosamine 6-phosphate recombinant enzyme, pH 7.4, 37°C Escherichia coli