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2,6-diaminopurine riboside
-
6-thio-GTP
the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
6-thioguanosine 5'-triphosphate
no guanosine, kact: 8.5/sec, KA: 0.035 mM, Ki: 0.27 mM
8-oxoguanosine 5'-triphosphate
-
acycloguanosine monophosphate
-
guanosine 5'-tetraphosphate
O-methylguanosine 5'-triphosphate
no guanosine, kact: 2.8/sec, KA: 0.13 mM, Ki: 0.29 mM
O6-methyl-GTP
the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
S-nitroso-L-cysteine
specific irreversible inhibitor,inhibits the activity by 94%
S-nitroso-L-homocysteine
specific irreversible inhibitor, inhibits the activity by 90%
1,3,7,9-tetramethyluric
-
-
1,3,7-trimethyluric acid
-
-
1,3-dimethyluric acid
-
pH-dependent inhibition, overview
1,7-dimethyluric acid
-
pH-dependent inhibition, overview
2',3'-dialdehyde adenosine 5'-triphosphate
irreversible inhibitor of CTPS
2-Thiocytidine 5'-triphosphate
-
-
2-thiouridine 5'-triphosphate
-
-
3,7-dimethyluric acid
-
-
4-thiouridine 5'-triphosphate
-
-
6-diazo-5-oxo-L-norleucine
-
-
Cu2+
-
inhibition is not reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM
D,L-2-amino-4-phosphonobutyrate
-
-
DELTA1-Pyrroline-5-carboxylate
-
weak
glutamate gamma-semialdehyde
-
potent linear mixed-type inhibitor, competitive with respect to ammonia, no inhibition of the mutant enzyme C379A
L-2-pyrrolidone 5-carboxylate
-
weak competitive inhibition of the reaction with ammonia as substrate, no significant inhibition with glutamine as substrate
Ni2+
-
in presence of dithiothreitol inhibition at concentrations below 0.2 mM
paraxanthine
-
pH-dependent inhibition, overview
pyrrole-2-carboxylate
-
weak competitive inhibition of the reaction with ammonia as substrate, no significant inhibition with glutamine as substrate
theophylline
-
pH-dependent inhibition, overview
uric acid
-
pH-dependent inhibition, overview
Zn2+
-
inhibition is reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM
2'-deoxy-GTP
no guanosine, kact: 1.5/sec, KA: 0.21 mM, Ki: 0.36 mM
2'-deoxy-GTP
the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
GTP
0.1 mM guanosine, kact: 10.3/sec, KA: 0.088 mM, Ki: 0.22 mM
GTP
0.2 mM guanosine, kact: 8.2/sec, KA: 0.078 mM, Ki: 0.12 mM
GTP
no guanosine, kact: 10.6/sec, KA: 0.081 mM, Ki: 0.28 mM
GTP
allosteric effector, structural requirements for activation are stringent, but requirements for inhibition are lax. GTP promotes Gln hydrolysis but inhibits Gln-dependent CTP formation at concentrations of over 0.15 mM
guanosine 5'-tetraphosphate
-
guanosine 5'-tetraphosphate
no guanosine, kact: 4/sec, KA: 0.19 mM, Ki: 0.5 mM
guanosine 5'-tetraphosphate
the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
ITP
no guanosine, kact: 5.2/sec, KA: 2.9 mM, Ki: 4.5 mM
ITP
the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
CTP
-
-
GTP
-
inhibition of glutamine-dependent CTP formation above 0.15 mM, inhibition of glutamine-dependent CTP formation in a concentration-dependent manner
GTP
-
GTP acts a positive allosteric effector for Gln-dependent CTP formation. However, at concentrations exceeding 0.15 mM, GTP inhibits Gln-dependent CTP formation. Moreover, GTP is an inhibitor of NH3-dependent CTP formation at all concentrations
xanthine
-
-
xanthine
-
pH-dependent inhibition, overview
additional information
incubation of EcCTPS modified by CysNO and HcyNO with 5 mM DTT for 30 min at 37°C reveals that 88% and 97%, respectively, of the original activity can be recovered
-
additional information
it is shown that in the presence of 1 mM Gln, S-nitroso-L-cysteine reduces the enzymatic activity by 88% and by 32% in the presence of 10 mM Gln. Similar studies with S-nitroso-L-homocysteine result in reduction of the activity by 43% and 19%, respectively. The results suggest that the substrate Gln competitively protects the active site of EcCTPS from the modification with S-nitroso-L-cysteine and S-nitroso-L-homocysteine.
-
additional information
no inhibition by S-nitrosoglutathione presumably due to its inability to enter the actve site of the enzyme
-
additional information
GTP analogues inhibite NH3-and Gln-dependent CTP-formation, often in a cooperative manner, to a similar extent as they activate it with IC50 values of 0.2-0.5 mM, the inhibition appears to be due solely to the purine base, binding structures and kinetics, overview. Inhibitor structure-activity study, overview
-
additional information
-
GTP analogues inhibite NH3-and Gln-dependent CTP-formation, often in a cooperative manner, to a similar extent as they activate it with IC50 values of 0.2-0.5 mM, the inhibition appears to be due solely to the purine base, binding structures and kinetics, overview. Inhibitor structure-activity study, overview
-
additional information
-
enzyme loses activity at ionic strengths higher than 0.4 M
-
additional information
-
inhibition by xanthine and derivatives, no inhibition by allantoin, an intact purine ring with anionic character favors inhibition. In general, methylation of the purine does not significantly affect inhibition
-
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6-thio-GTP
the GTP analogue is capable of activating Gln-dependent CTP formation
6-thioguanosine 5'-triphosphate
0 mM guanosine, kact: 8.5/sec, KA: 0.035 mM, Ki: 0.27 mM
guanosine 5'-tetraphosphate
O-methylguanosine 5'-triphosphate
0 mM guanosine, kact: 2.8/sec, KA: 0.13 mM, Ki: 0.29 mM
O6-methyl-GTP
the GTP analogue is capable of activating Gln-dependent CTP formation
2'-deoxy-GTP
0 mM guanosine, kact: 1.5/sec, KA: 0.21 mM, Ki: 0.36 mM
2'-deoxy-GTP
the GTP analogue is capable of activating Gln-dependent CTP formation
GTP
0 mM guanosine, kact: 10.6/sec, KA: 0.081 mM, Ki: 0.28 mM
GTP
0.1 mM guanosine, kact: 10.3/sec, KA: 0.088 mM, Ki: 0.22 mM
GTP
0.2 mM guanosine, kact: 8.2/sec, KA: 0.078 mM, Ki: 0.12 mM
GTP
allosteric effector, structural requirements for activation are stringent, but requirements for inhibition are lax. GTP promotes Gln hydrolysis but inhibits Gln-dependent CTP formation at concentrations of over 0.15 mM
guanosine 5'-tetraphosphate
0 mM guanosine, kact: 4/sec, KA: 0.19 mM, Ki: 0.5 mM
guanosine 5'-tetraphosphate
the GTP analogue is capable of activating Gln-dependent CTP formation
ITP
0 mM guanosine, kact: 5.2/sec, KA: 2.9 mM, Ki: 4.5 mM
ITP
the GTP analogue is capable of activating Gln-dependent CTP formation
GTP
-
required as allosteric effector to promote reaction with glutamine as substrate, GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis
GTP
-
required as an allosteric effector to promote glutamine hydrolysis
GTP
-
activates enzyme-catalyzed glutamine hydrolysis
GTP
-
GTP acts a positive allosteric effector for Gln-dependent CTP formation. However, at concentrations exceeding 0.15 mM, GTP inhibits Gln-dependent CTP formation. Moreover, GTP is an inhibitor of NH3-dependent CTP formation at all concentrations
additional information
activation potency in descending order: GTP = 6-thio-GTP, ITP = guanosine 5'-tetraphosphate, O6-methyl-GTP, 2'-deoxy-GTP, no activation with guanosine, GMP, GDP, 2',3'-dideoxy-GTP, acycloguanosine, and acycloguanosine monophosphate, indicating that the 5'-triphosphate, 2'-OH, and 3'-OH are required for full activation, binding structures and kinetics, overview
-
additional information
-
activation potency in descending order: GTP = 6-thio-GTP, ITP = guanosine 5'-tetraphosphate, O6-methyl-GTP, 2'-deoxy-GTP, no activation with guanosine, GMP, GDP, 2',3'-dideoxy-GTP, acycloguanosine, and acycloguanosine monophosphate, indicating that the 5'-triphosphate, 2'-OH, and 3'-OH are required for full activation, binding structures and kinetics, overview
-
additional information
binding of the substrates ATP and UTP, or the product CTP, promotes oligomerization of CTPS from inactive dimers to active tetramers, Gly142 is critical for nucleotide-dependent oligomerization of CTPS to active tetramers
-
additional information
-
binding of the substrates ATP and UTP, or the product CTP, promotes oligomerization of CTPS from inactive dimers to active tetramers, Gly142 is critical for nucleotide-dependent oligomerization of CTPS to active tetramers
-
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39.4
L-glutamine
37°C, pH 8.0, wild-type enzyme
0.054
ATP
-
pH 8.0, 25°C, without GTP
additional information
additional information
-
0.354
Gln
37°C, pH 8.0, wild-type enzyme
0.497
Gln
37°C, pH 8.0, mutant enzyme L109A
0.063
Gln-OH
37°C, pH 8.0, mutant enzyme L109A
0.165
Gln-OH
37°C, pH 8.0, wild-type enzyme
75.3
NH2OH
37°C, pH 8.0, mutant enzyme L109A
82.8
NH2OH
37°C, pH 8.0, wild-type enzyme
2.15
NH3
37°C, pH 8.0, wild-type enzyme
2.17
NH3
37°C, pH 8.0, mutant enzyme L109A
0.196
glutamine
mutant K306A, presence of 1 mM ATP, 1 mM UTP
0.206
glutamine
wild-type protein, presence of 3 mM ATP, 2 mM UTP
0.345
glutamine
wild-type protein, presence of 1 mM ATP, 1 mM UTP
0.424
glutamine
mutant K306A, presence of 3 mM ATP, 2 mM UTP
0.627
NH3
mutant K306A, presence of 1 mM ATP, 1 mM UTP
1.47
NH3
mutant K306A, presence of 3 mM ATP, 2 mM UTP
1.54
NH3
mutant K297A, presence of 1 mM ATP, 1 mM UTP
2.15
NH3
wild-type protein, presence of 1 mM ATP, 1 mM UTP
2.79
NH3
wild-type protein, presence of 3 mM ATP, 2 mM UTP
0.027
UTP
-
pH 8.0, 25°C, without GTP
0.071
UTP
-
pH 8.0, 25°C, activation with GTP
additional information
additional information
kinetic mechanism, activation and inhibition kinetics
-
additional information
additional information
-
kinetic mechanism, activation and inhibition kinetics
-
additional information
additional information
kinetics of wild-type and mutants
-
additional information
additional information
-
kinetics of wild-type and mutants
-
additional information
additional information
-
positive cooperativity for ATP and UTP
-
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1.5
2'-deoxy-GTP
no guanosine
8.5
6-thioguanosine 5'-triphosphate
no guanosine, kact: 8.5/sec, KA: 0.035 mM, Ki: 0.27 mM
4
guanosine 5'-tetraphosphate
no guanosine
1.41
L-glutamine
37°C, pH 8.0, wild-type enzyme
2.8
O-methylguanosine 5'-triphosphate
no guanosine
0.0058 - 0.054
2',3'-dialdehyde adenosine 5'-triphosphate
additional information
additional information
-
-
-
1.86
Gln
37°C, pH 8.0, mutant enzyme L109A
6.1
Gln
37°C, pH 8.0, wild-type enzyme
0.063
Gln-OH
37°C, pH 8.0, mutant enzyme L109A
0.453
Gln-OH
37°C, pH 8.0, wild-type enzyme
8.2
GTP
0.2 mM guanosine
10.3
GTP
0.1 mM guanosine
14
NH2OH
37°C, pH 8.0, wild-type enzyme
14.1
NH2OH
37°C, pH 8.0, mutant enzyme L109A
9.5
NH3
37°C, pH 8.0, wild-type enzyme
10.1
NH3
37°C, pH 8.0, mutant enzyme L109A
0.08
UTP
pH 8.0, 37°C, mutant G142A with L-glutamine, in presence of 0.25 mM GTP
0.67
UTP
pH 8.0, 37°C, mutant G143A with L-glutamine, in presence of 0.25 mM GTP
4.2
UTP
pH 8.0, 37°C, mutant G146A with L-glutamine, in presence of 0.25 mM GTP
5
UTP
pH 8.0, 37°C, wild-type enzyme with L-glutamine, in presence of 0.25 mM GTP
0.0058
2',3'-dialdehyde adenosine 5'-triphosphate
K306A: replacement of lysine 306 by alanine reduces the rate of 2',3'-dialdehyde adenosine 5'-triphosphate-dependent inactivation
0.054
2',3'-dialdehyde adenosine 5'-triphosphate
in the presence of 10 mM UTP
6.26
ATP
K306A, presence of 2 mM UTP
10.8
ATP
K297A, presence of 2 mM UTP
12.8
ATP
wild-type protein, presence of 2 mM UTP
1.03
Gln
-
pH 8.0, mutant enzyme L109F
1.53
Gln
-
pH 8.0, mutant enzyme R105A
1.64
Gln
-
pH 8.0, mutant enzyme L109A
2.17
Gln
-
pH 8.0, mutant enzyme G110A
3.5
Gln
-
pH 8.0, mutant enzyme D107A
4.22
Gln
-
pH 8.0, mutant enzyme K102A
6.1
Gln
-
pH 8.0, wild-type enzyme
0.233
glutamine
-
reaction without GTP
1.28
glutamine
mutant K306A, presence of 1 mM ATP, 1 mM UTP
1.35
glutamine
mutant K306A, presence of 3 mM ATP, 2 mM UTP
1.5
glutamine
wild-type protein, presence of 3 mM ATP, 2 mM UTP
6.1
glutamine
wild-type protein, presence of 1 mM ATP, 1 mM UTP
6.7
glutamine
-
pH 8.0, wild-type enzyme
8.1
glutamine
-
pH 8.0, recombinant His6-tagged enzyme
0.031 - 0.51
NH3
mutant K306A, presence of 3 mM ATP, 2 mM UTP
0.18
NH3
-
pH 8.0, mutant enzyme H118A
0.92
NH3
-
pH 8.0, mutant enzyme E103A
1.96
NH3
-
pH 8.0, mutant enzymeR104A
2.19
NH3
mutant K306A, presence of 1 mM ATP, 1 mM UTP
2.25
NH3
-
reaction with or without GTP
4.18
NH3
-
pH 8.0, mutant enzyme G110A
7.59
NH3
mutant K306A, presence of 3 mM ATP, 2 mM UTP
7.97
NH3
-
pH 8.0, mutant enzyme L109A
8.59
NH3
mutant K297A, presence of 1 mM ATP, 1 mM UTP
8.7
NH3
-
pH 8.0, mutant enzyme D107A
8.88
NH3
-
pH 8.0, mutant enzyme R105A
9.4
NH3
-
pH 8.0, wild-type enzyme
9.5
NH3
wild-type protein, presence of 1 mM ATP, 1 mM UTP
9.9
NH3
-
pH 8.0, mutant enzyme C379A
10.4
NH3
-
pH 8.0, mutant enzyme C379S
11
NH3
-
pH 8.0, mutant enzyme L109F
11.3
NH3
wild-type protein, presence of 3 mM ATP, 2 mM UTP
12.2
NH3
-
pH 8.0, mutant enzyme K102A
6.9
UTP
K306A, presence of 2 mM ATP
13.7
UTP
wild-type protein, presence of 3 mM ATP
14
UTP
K297A, presence of 3 mM ATP
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0.27
6-thioguanosine 5'-triphosphate
-
0.5
guanosine 5'-tetraphosphate
-
0.29
O-methylguanosine 5'-triphosphate
-
0.027
S-nitroso-L-cysteine
Kinact: 0.48/min
0.33
1-beta-D-ribofuranosyl-2-thiouracil 5'-triphosphate
-
pH 7.2, inhibition of glutamine reaction
3.36 - 3.7
2',3'-dialdehyde adenosine 5'-triphosphate
0.08
2-Thiocytidine 5'-triphosphate
-
pH 7.2, inhibition of glutamine reaction and ammonia reaction
0.1 - 0.25
2-thiouridine 5'-triphosphate
5.6
D,L-2-amino-4-phosphonobutyrate
-
pH 8.0, reaction with ammonia
0.39
glutamate gamma-semialdehyde
-
-
12.6
L-2-pyrrolidone-5-carboxylate
-
pH 8.0, reaction with ammonia
11
pyrrole-2-carboxylate
-
pH 8.0, reaction with ammonia
0.51
s4UTP
-
pH 7.2, inhibition of ammonia reaction
additional information
additional information
-
0.12
GTP
0.2 mM guanosine
0.22
GTP
0.1 mM guanosine
3.36
2',3'-dialdehyde adenosine 5'-triphosphate
in the presence of 10 mM UTP
3.7
2',3'-dialdehyde adenosine 5'-triphosphate
K306A: replacement of lysine 306 by alanine reduces the rate of 2',3'-dialdehyde adenosine 5'-triphosphate-dependent inactivation
0.1
2-thiouridine 5'-triphosphate
-
pH 7.2, inhibition of glutamine reaction
0.25
2-thiouridine 5'-triphosphate
-
pH 7.2, inhibition of ammonia reaction
0.18
5-bromoUTP
-
pH 7.2, inhibition of glutamine reaction
0.53
5-bromoUTP
-
pH 7.2, inhibition of ammonia reaction
0.08
CTP
-
pH 7.2, inhibition of glutamine reaction
0.09
CTP
-
pH 7.2, inhibition of ammonia reaction
additional information
additional information
no saturation kinetic is obtained with S-nitroso-L-homocysteine
-
additional information
additional information
nucleotide and nucleoside analogues of GTP and guanosine, respectively, all inhibit NH3- and Gln-dependent CTP formation to a similar extent (IC50 : 0.20.5 mM). This inhibition appears to be due solely to the purine base and is relatively insensitive to the identity of the purine with the exception of inosine, ITP, and adenosine (IC50 : 412 mM). 8-Oxoguanosine is the best inhibitor identified (IC50 : 0.08 mM).
-
additional information
additional information
-
nucleotide and nucleoside analogues of GTP and guanosine, respectively, all inhibit NH3- and Gln-dependent CTP formation to a similar extent (IC50 : 0.20.5 mM). This inhibition appears to be due solely to the purine base and is relatively insensitive to the identity of the purine with the exception of inosine, ITP, and adenosine (IC50 : 412 mM). 8-Oxoguanosine is the best inhibitor identified (IC50 : 0.08 mM).
-
additional information
additional information
kinetic mechanism, activation and inhibition kinetics
-
additional information
additional information
-
kinetic mechanism, activation and inhibition kinetics
-
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics. Multisite inhibition of CTPS-catalyzed NH3-dependent CTP formation by caffeine
-
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0.33 - 0.45
2'-deoxy-guanosine
0.11 - 0.18
2,6-diaminopurine riboside
0.22 - 0.26
2-aminopurine riboside
0.34 - 0.4
3'-deoxy-guanosine
0.39 - 0.61
6-thioguanine
0.23 - 0.4
6-thioguanosine
0.08 - 0.13
8-oxoguanosine
0.11 - 0.15
8-oxoguanosine 5'-triphosphate
0.33 - 0.49
acycloguanosine
0.31 - 0.41
acycloguanosine monophosphate
0.33 - 0.42
guanosine 5'-tetraphosphate
0.17 - 0.23
N-methylguanosine
0.15 - 0.25
O-methylguanosine
0.079 - 0.121
1,3,7,9-tetramethyluric
0.067 - 0.07
1,3,7-trimethyluric acid
0.072 - 0.088
1,3-dimethyluric acid
0.113 - 0.119
1,7-dimethyluric acid
0.096 - 0.101
1-methyluric acid
0.063 - 0.09
3,7-dimethyluric acid
0.15
CTP
Escherichia coli
-
IC50: 0.15 mM
2.6 - 3.2
uracil-4-acetic acid
additional information
additional information
Escherichia coli
-
xanthine and related compounds inhibit CTPS activity with IC50 = 0.16-0.58 mM. The presence of an 8-oxo function enhances the inhibition to IC50 = 0.060-0.121 mM. Raising the pH from 8.0 to 8.5 results in slightly increased inhibition of NH3-dependent CTP formation by the xanthines
-
0.33
2'-deoxy-GTP
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.42
2'-deoxy-GTP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.33
2'-deoxy-guanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.45
2'-deoxy-guanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.11
2,6-diaminopurine riboside
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.18
2,6-diaminopurine riboside
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.22
2-aminopurine riboside
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.26
2-aminopurine riboside
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.34
3'-deoxy-guanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.4
3'-deoxy-guanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.39
6-thioguanine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.61
6-thioguanine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.23
6-thioguanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.4
6-thioguanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.08
8-oxoguanosine
Escherichia coli
-
0.08
8-oxoguanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.13
8-oxoguanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.11
8-oxoguanosine 5'-triphosphate
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.15
8-oxoguanosine 5'-triphosphate
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.33
acycloguanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.45
acycloguanosine
Escherichia coli
8.16 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.45
acycloguanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.47
acycloguanosine
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.48
acycloguanosine
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.49
acycloguanosine
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.31
acycloguanosine monophosphate
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.41
acycloguanosine monophosphate
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
11
adenosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
12
adenosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.29
dideoxy-GTP
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.41
dideoxy-GTP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.29
GDP
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.29
GDP
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.29
GDP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.3
GDP
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.33
GDP
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.23
GMP
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.25
GMP
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.26
GMP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.28
GMP
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.29
GMP
Escherichia coli
8.16 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.33
GMP
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.29
GTP
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.3
GTP
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.3
GTP
Escherichia coli
8.16 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.3
GTP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.31
GTP
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.22
guanosine
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.26
guanosine
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.26
guanosine
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.29
guanosine
Escherichia coli
8.16 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
0.29
guanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.3
guanosine
Escherichia coli
0.30 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.32
guanosine
Escherichia coli
10 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.32
guanosine
Escherichia coli
2.5 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.32
guanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.35
guanosine
Escherichia coli
0.75 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.33
guanosine 5'-tetraphosphate
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.42
guanosine 5'-tetraphosphate
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
3.5
Inosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
5.2
Inosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
2.9
ITP
Escherichia coli
8.16 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
3
ITP
Escherichia coli
2.72 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
3.1
ITP
Escherichia coli
5.44 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
3.3
ITP
Escherichia coli
1.36 mM NH3, IC50 for inhibition of NH3-dependent CTP formation
3.7
ITP
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
4.1
ITP
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.17
N-methylguanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.23
N-methylguanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.15
O-methylguanosine
Escherichia coli
0.30 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.16
O-methylguanosine
Escherichia coli
10 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.16
O-methylguanosine
Escherichia coli
2.5 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.16
O-methylguanosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.17
O-methylguanosine
Escherichia coli
0.75 mM Gln, IC50 for inhibition of Gln-dependent CTP formation
0.25
O-methylguanosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.22
Xanthosine
Escherichia coli
IC50 for inhibition of Gln-dependent CTP formation
0.29
Xanthosine
Escherichia coli
IC50 for inhibition of NH3-dependent CTP formation
0.079
1,3,7,9-tetramethyluric
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.121
1,3,7,9-tetramethyluric
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.067
1,3,7-trimethyluric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.07
1,3,7-trimethyluric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.072
1,3-dimethyluric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.088
1,3-dimethyluric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.113
1,7-dimethyluric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.119
1,7-dimethyluric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.096
1-methyluric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.101
1-methyluric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.063
3,7-dimethyluric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.09
3,7-dimethyluric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
12.9
adenine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
15.8
adenine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.39
Caffeine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.51
Caffeine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.44
paraxanthine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.48
paraxanthine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.42
Theobromine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.58
Theobromine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.43
theophylline
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.55
theophylline
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
4.2
Uracil
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
4.7
Uracil
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
2.6
uracil-4-acetic acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
3.2
uracil-4-acetic acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.06
uric acid
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.087
uric acid
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
3.1
uridine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
4.6
uridine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.23
xanthine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.37
xanthine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
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G142A
site-directed mutagenesis, inactive mutant with both ammonia and glutamine
G143A
site-directed mutagenesis, kcat/Km for ammonia-dependent and glutamine-dependent CTP formation by mutant G143A are reduced by 22fold and 16fold, respectively, compared to the wild-type enzyme. The mutant is able to form active tetramers in the presence of ATP and UTP
G146A
site-directed mutagenesis, kcat/Km for ammonia-dependent and glutamine-dependent CTP formation by mutant G143A are reduced by 1.4fold and 1.8fold, respectively, compared to the wild-type enzyme. The mutant is able to form active tetramers in the presence of ATP and UTP
L109A
uncoupling of the hydrolysis of gamma-glutamyl hydroxamate and nascent NH2OH production from N4-hydroxy-CTP formation is more pronounced with mutant than with wild-type enzyme
C379A
-
mutant enzyme is fully active with ammonia but has no glutamine-dependent activity, no inhibition by glutamate gamma-semialdehyde
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
E103A
-
mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3
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
G351A
-
mutation increases lability of the enzyme, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation
G352C
-
mutation increases lability of the enzyme, mutation abolishes the capacity to form the covalent glutaminyl-cysteine379 catalytic intermediate, thus preventing glutamine amide transfer function, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation
G352P
-
mutation increases lability of the enzyme, mutation abolishes the capacity to form the covalent glutaminyl-cysteine379 catalytic intermediate, thus preventing glutamine amide transfer function, mutant enzyme is not overproduced because of apparent instability and proteolytic degradation
H118A
-
mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3
K102A
-
mutant enzyme exhibits wild-type activity with respect to NH3 and glutamine
K297A
replacement of lysine 297 by alanine does not affect NH3-dependent CTP formation, relative to wild-type CTPS, but reduces kcat for the glutaminase activity 78fold
K306A
replacement of lysine 306 by alanine reduces the rate of 2',3'-dialdehyde adenosine 5'-triphosphate-dependent inactivation (Kinact = 0.0058/sec, Ki = 3.7 mM) and reduces the apparent affinity for CTPS for both ATP and UTP by 2fold. The efficiency of K306A-catalyzed glutamine-dependent CTP formation is also reduced 2fold while near wild type activity is observed when NH3 is the substrate. These findings suggest that Lys 206 is not essential for ATP binding, but does play a role in bringing about the conformational changes that mediate interactions between ATP and UTP sites, and between the ATP-binding site and the glutamine amide transfer domain
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
R104A
-
mutant enzyme exhibits no glutamine-dependent activity and is only partially active with NH3
R105A
-
enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation
V349S
-
mutation increases lability of the enzyme
additional information
it can be suggested that the conformational change associated with binding ATP may be transmitted through the L10-alpha11 structural unit (residues 297-312) and thereby mediate effects on the glutaminase activity of CTPS
additional information
-
it can be suggested that the conformational change associated with binding ATP may be transmitted through the L10-alpha11 structural unit (residues 297-312) and thereby mediate effects on the glutaminase activity of CTPS
additional information
-
Escherichia coli CtpS can replace the enzymatic and morphogenic functions of Caulobacter crescentus CtpS
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Iyengar, A.; Bearne, S.L.
Aspartate-107 and leucine-109 facilitate efficient coupling of glutamine hydrolysis to CTP synthesis by Escherichia coli CTP synthase
Biochem. J.
369
497-507
2003
Escherichia coli
brenda
Bearne, S.L.; Hekmat, O.; Macdonnell, J.E.
Inhibition of Escherichia coli CTP synthase by glutamate gamma-semialdehyde and the role of the allosteric effector GTP in glutamine hydrolysis
Biochem. J.
356
223-232
2001
Escherichia coli
brenda
van Kuilenburg, A.B.; Meinsma, R.; Vreken, P.; Waterham, H.R.; van Gennip, A.H.
Identification of a cDNA encoding an isoform of human CTP synthetase
Biochim. Biophys. Acta
1492
548-552
2000
Escherichia coli (P0A7E5), Escherichia coli, Homo sapiens (P17812), Homo sapiens (Q9NRF8), Homo sapiens, Saccharomyces cerevisiae (P28274), Saccharomyces cerevisiae (P38627), Mus musculus (P70303), Mus musculus (P70698)
brenda
Weng, M.; Zalkin, H.
Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain
J. Bacteriol.
169
3023-3028
1987
Escherichia coli
brenda
Zalkin, H.
CTP synthetase
Methods Enzymol.
113
282-287
1985
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
von der Saal, W.; Villafranca, J.J.; Anderson, P.M.
Cytidine-5'-triphosphate synthetase catalyzes the phosphorylation of uridine 5'-triphosphate by adenosine 5'-triphosphate
J. Am. Chem. Soc.
107
703-704
1985
Chlamydia trachomatis, Escherichia coli
-
brenda
Anderson, P.M.
CTP synthetase from Escherichia coli: an improved purification procedure and characterization of hysteretic and enzyme concentration effects on kinetic properties
Biochemistry
22
3285-3292
1983
Escherichia coli
brenda
Scheit, K.H.; Linke, H.J.
Substrate specificity of CTP synthetase from Escherichia coli
Eur. J. Biochem.
126
57-60
1982
Escherichia coli
brenda
Long, C.; Koshland jr., D.E.
Cytidine triphosphate synthetase
Methods Enzymol.
51
79-83
1978
Escherichia coli
brenda
Koshland jr., D.E.; Levitzki, A.
CTP synthetase and related enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
539-559
1974
Escherichia coli
-
brenda
Scheit, K.H.; Linke, H.J.
Substrate specificity of CTP synthetase from E. coli
Nucleic Acids Res.
9
229-233
1981
Escherichia coli
brenda
Lewis, D.A.; Villafranca, J.J.
Investigation of the mechanism of CTP synthetase using rapid quench and isotope partitioning methods
Biochemistry
28
8454-8459
1989
Escherichia coli
brenda
Wylie, J.L.; Berry, J.D.; McClarty, G.
Chlamydia trachomatis CTP synthetase: molecular characterization and developmental regulation of expression
Mol. Microbiol.
22
631-642
1996
Chlamydia trachomatis, Escherichia coli
brenda
Robertson, J.G.; Villafranca, J.J.
Characterization of metal ion activation and inhibition of CTP synthetase
Biochemistry
32
3769-3777
1993
Escherichia coli
brenda
Endrizzi, J.A.; Kim, H.; Anderson, P.M.; Baldwin, E.P.
Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets
Biochemistry
43
6447-6463
2004
Escherichia coli (P0A7E5), Escherichia coli
brenda
MacDonnell, J.E.; Lunn, F.A.; Bearne, S.L.
Inhibition of E. coli CTP synthase by the "positive" allosteric effector GTP
Biochim. Biophys. Acta
1699
213-220
2004
Escherichia coli
brenda
Lunn, F.A.; Bearne, S.L.
Alternative substrates for wild-type and L109A E. coli CTP synthases: kinetic evidence for a constricted ammonia tunnel
Eur. J. Biochem.
271
4204-4212
2004
Escherichia coli (P0A7E5), Escherichia coli
brenda
MacLeod, T.J.; Lunn, F.A.; Bearne, S.L.
The role of lysine residues 297 and 306 in nucleoside triphosphate regulation of E. coli CTP synthase: inactivation by 2,3-dialdehyde ATP and mutational analyses
Biochim. Biophys. Acta
1764
199-210
2006
Escherichia coli (A0A140N932), Escherichia coli
brenda
Lunn, F.A.; Macdonnell, J.E.; Bearne, S.L.
Structural requirements for the activation of Escherichia coli CTP synthase by the allosteric effector GTP are stringent, but requirements for inhibition are Lax
J. Biol. Chem.
283
2010-2020
2007
Escherichia coli (P0A7E5), Escherichia coli
brenda
Braun, O.; Knipp, M.; Chesnov, S.; Vasak, M.
Specific reactions of S-nitrosothiols with cysteine hydrolases: A comparative study between dimethylargininase-1 and CTP synthetase
Protein Sci.
16
1522-1534
2007
Escherichia coli (P0A7E5)
brenda
Lunn, F.A.; Macleod, T.J.; Bearne, S.L.
Mutational analysis of conserved glycine residues 142, 143 and 146 reveals Gly(142) is critical for tetramerization of CTP synthase from Escherichia coli
Biochem. J.
412
113-121
2008
Escherichia coli (P0A7E5), Escherichia coli
brenda
Roy, A.C.; Lunn, F.A.; Bearne, S.L.
Inhibition of CTP synthase from Escherichia coli by xanthines and uric acids
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20
141-144
2010
Escherichia coli
brenda
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The metabolic enzyme CTP synthase forms cytoskeletal filaments
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12
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2010
Caulobacter vibrioides, Escherichia coli
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