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Literature summary for 2.6.1.16 extracted from

  • Floquet, N.; Mouilleron, S.; Daher, R.; Maigret, B.; Badet, B.; Badet-Denisot, M.A.
    Ammonia channeling in bacterial glucosamine-6-phosphate synthase (Glms): molecular dynamics simulations and kinetic studies of protein mutants (2007), FEBS Lett., 581, 2981-2987.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations. Key role for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer Escherichia coli

Protein Variants

Protein Variants Comment Organism
A602L enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure Escherichia coli
V605L enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure Escherichia coli
W74A enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure Escherichia coli
W74A efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate Escherichia coli
W74F enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure Escherichia coli
W74L enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure Escherichia coli
W74L decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0064
-
L-gamma-glutamyl-p-nitroanilide mutant W74F, 37°C Escherichia coli
0.04
-
L-glutamine mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.04
-
L-glutamine mutant W74L, 37°C Escherichia coli
0.048
-
L-glutamine mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.048
-
L-glutamine mutant W74F, 37°C Escherichia coli
0.05
-
L-gamma-glutamyl-p-nitroanilide wild-type, 37°C Escherichia coli
0.072
-
L-glutamine mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.072
-
L-glutamine mutant V605L, 37°C Escherichia coli
0.1
-
L-glutamine mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.1
-
L-glutamine mutant A602L, 37°C Escherichia coli
0.1
-
L-gamma-glutamyl-p-nitroanilide mutant W74L, 37°C Escherichia coli
0.2
-
L-gamma-glutamyl-p-nitroanilide mutant W74A, 37°C Escherichia coli
0.27
-
L-glutamine wild-type, 37°C Escherichia coli
0.27
-
L-glutamine wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.29
-
L-gamma-glutamyl-p-nitroanilide mutant V605L, 37°C Escherichia coli
0.36
-
D-fructose 6-phosphate wild-type, 37°C Escherichia coli
0.36
-
D-fructose 6-phosphate wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.36
-
L-gamma-glutamyl-p-nitroanilide mutant A602L, 37°C Escherichia coli
0.38
-
L-glutamine mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.38
-
L-glutamine mutant W74A, 37°C Escherichia coli
0.67
-
D-fructose 6-phosphate mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.67
-
D-fructose 6-phosphate mutant V605L, 37°C Escherichia coli
0.93
-
D-fructose 6-phosphate mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.93
-
D-fructose 6-phosphate mutant W74A, 37°C Escherichia coli
1.11
-
D-fructose 6-phosphate mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
1.11
-
D-fructose 6-phosphate mutant W74L, 37°C Escherichia coli
1.15
-
D-fructose 6-phosphate mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
1.15
-
D-fructose 6-phosphate mutant A602L, 37°C Escherichia coli
1.45
-
D-fructose 6-phosphate mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
1.45
-
D-fructose 6-phosphate mutant W74F, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P17169
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose fast flow column chromatography and Superdex 200 HR 26/60 Hiload gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 6-phosphate determination of hexose phosphate-isomerizing activity Escherichia coli D-glucose 6-phosphate
-
?
L-gamma-glutamyl-p-nitroanilide + H2O determination of amidohydrolysing activity Escherichia coli L-glutamine + p-nitroaniline
-
?
L-glutamine + D-fructose 6-phosphate
-
Escherichia coli L-glutamate + D-glucosamine 6-phosphate
-
?

Synonyms

Synonyms Comment Organism
GlmS
-
Escherichia coli
glucosamine-6-P synthase
-
Escherichia coli
glucosamine-6-phosphate synthase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
D-fructose 6-phosphate mutant W74L, 37°C Escherichia coli
0.083
-
D-fructose 6-phosphate mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.12
-
D-fructose 6-phosphate mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.12
-
D-fructose 6-phosphate mutant W74A, 37°C Escherichia coli
0.13
-
L-gamma-glutamyl-p-nitroanilide mutant V605L, 37°C Escherichia coli
0.15
-
D-fructose 6-phosphate mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.15
-
L-gamma-glutamyl-p-nitroanilide mutant A602L, 37°C Escherichia coli
0.15
-
D-fructose 6-phosphate mutant V605L, 37°C Escherichia coli
0.17
-
L-gamma-glutamyl-p-nitroanilide wild-type, 37°C Escherichia coli
0.22
-
D-fructose 6-phosphate mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.22
-
D-fructose 6-phosphate mutant A602L, 37°C Escherichia coli
0.28
-
L-glutamine mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.28
-
L-glutamine mutant V605L, 37°C Escherichia coli
0.38
-
L-glutamine mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.38
-
L-glutamine mutant A602L, 37°C Escherichia coli
0.5
-
L-gamma-glutamyl-p-nitroanilide mutant W74L, 37°C Escherichia coli
0.52
-
D-fructose 6-phosphate wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.67
-
L-gamma-glutamyl-p-nitroanilide mutant W74F, 37°C Escherichia coli
0.68
-
L-gamma-glutamyl-p-nitroanilide mutant W74A, 37°C Escherichia coli
0.92
-
D-fructose 6-phosphate mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
0.92
-
D-fructose 6-phosphate mutant W74F, 37°C Escherichia coli
0.97
-
L-glutamine wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
1.5
-
L-glutamine mutant W74L, 37°C Escherichia coli
1.55
-
L-glutamine mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
3
-
L-glutamine mutant W74A, 37°C Escherichia coli
3.02
-
L-glutamine mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
7.17
-
L-glutamine mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
7.2
-
L-glutamine mutant W74F, 37°C Escherichia coli
14.4
-
D-fructose 6-phosphate wild-type, 37°C Escherichia coli
14.42
-
D-fructose 6-phosphate wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
17.17
-
L-glutamine wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C Escherichia coli
17.2
-
L-glutamine wild-type, 37°C Escherichia coli