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Literature summary for 6.3.4.2 extracted from

  • Iyengar, A.; Bearne, S.L.
    Aspartate-107 and leucine-109 facilitate efficient coupling of glutamine hydrolysis to CTP synthesis by Escherichia coli CTP synthase (2003), Biochem. J., 369, 497-507.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.4.2

Activating Compound

Activating Compound Comment Organism Structure
GTP required as an allosteric effector to promote glutamine hydrolysis Escherichia coli

Protein Variants

Protein Variants Comment Organism
D107A enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation, affinity of the mutant enzyme for GTP is reduced 2-4fold Escherichia coli
E103A mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3 Escherichia coli
G110A affinity of the mutant enzyme for GTP is reduced 2-4fold, enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation Escherichia coli
H118A mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3 Escherichia coli
K102A mutant enzyme exhibits wild-type activity with respect to NH3 and glutamine Escherichia coli
L109A enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation, affinity of the mutant enzyme for GTP is reduced 2-4fold Escherichia coli
R104A mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3 Escherichia coli
R105A enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + glutamine
-
 Escherichia coli ADP + phosphate + CTP + Glu
-
 ?
ATP + UTP + NH4+
-
 Escherichia coli ADP + phosphate + CTP
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.18
-
 NH3 pH 8.0, mutant enzyme H118A Escherichia coli
0.92
-
 NH3 pH 8.0, mutant enzyme E103A Escherichia coli
1.03
-
 Gln pH 8.0, mutant enzyme L109F Escherichia coli
1.53
-
 Gln pH 8.0, mutant enzyme R105A Escherichia coli
1.64
-
 Gln pH 8.0, mutant enzyme L109A Escherichia coli
1.96
-
 NH3 pH 8.0, mutant enzymeR104A Escherichia coli
2.17
-
 Gln pH 8.0, mutant enzyme G110A Escherichia coli
3.5
-
 Gln pH 8.0, mutant enzyme D107A Escherichia coli
4.18
-
 NH3 pH 8.0, mutant enzyme G110A Escherichia coli
4.22
-
 Gln pH 8.0, mutant enzyme K102A Escherichia coli
6.1
-
 Gln pH 8.0, wild-type enzyme Escherichia coli
7.97
-
 NH3 pH 8.0, mutant enzyme L109A Escherichia coli
8.7
-
 NH3 pH 8.0, mutant enzyme D107A Escherichia coli
8.88
-
 NH3 pH 8.0, mutant enzyme R105A Escherichia coli
9.4
-
 NH3 pH 8.0, wild-type enzyme Escherichia coli
11
-
 NH3 pH 8.0, mutant enzyme L109F Escherichia coli
12.2
-
 NH3 pH 8.0, mutant enzyme K102A Escherichia coli