Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.6.1.16 extracted from

  • Valerio-Lepiniec, M.; Aumont-Nicaise, M.; Roux, C.; Raynal, B.; England, P.; Badet, B.; Badet-Denisot, M.A.; Desmadril, M.
    Analysis of the Escherichia coli glucosamine-6-phosphate synthase activity by isothermal titration calorimetry and differential scanning calorimetry (2010), Arch. Biochem. Biophys., 498, 95-104.
    View publication on PubMed
Search for more literature for 2.6.1.16

Protein Variants

Protein Variants Comment Organism
C1A C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 L-glutamate calorimetric determination, pH 7.2, 25°C Escherichia coli
0.23
-
 D-fructose 6-phosphate calorimetric determination, pH 7.2, 37°C Escherichia coli
0.3
-
 D-fructose 6-phosphate calorimetric determination, pH 7.2, 25°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66640
-
 SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + D-fructose 6-phosphate
-
 Escherichia coli L-glutamate + D-glucosamine 6-phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form Escherichia coli
oligomer sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form Escherichia coli

Synonyms

Synonyms Comment Organism
GlmS in the absence of D-fructose 6-phosphate, the enzyme exhibits a weak hydrolyzing activity of Gln into Glu and ammonia (glutaminase activity), whereas the presence of D-fructose 6-phosphate strongly stimulates its hemisynthase activity Escherichia coli
glucosamine-6-phosphate synthase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.81
-
 L-glutamate calorimetric determination, pH 7.2, 25°C Escherichia coli
9.9
-
 D-fructose 6-phosphate calorimetric determination, pH 7.2, 25°C Escherichia coli
12
-
 D-fructose 6-phosphate calorimetric determination, pH 7.2, 37°C Escherichia coli