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ATP + dUTP + NH4+
ADP + phosphate + dCTP
ATP + UTP + CH3NHOH
ADP + phosphate + ?
-
-
-
-
?
ATP + UTP + gamma-L-glutamylhydroxamate
ADP + phosphate + N4-hydroxy-CTP
-
-
-
?
ATP + UTP + Gln
ADP + phosphate + CTP + Glu
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
ATP + UTP + glutamine
ADP + phosphate + CTP + L-glutamate
ATP + UTP + hydroxylamine
ADP + phosphate + N4-hydroxyCTP
-
activity is about 3fold higher than activity with NH4+
-
?
ATP + UTP + hydroxylamine
ADP + phosphate + N4-OH-CTP
-
-
-
-
?
ATP + UTP + L-gamma-glutamyl hydrazide
ADP + phosphate + N4-amino-CTP + L-glutamate
-
-
-
?
ATP + UTP + L-Gln
ADP + phosphate + CTP + L-Glu
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
ATP + UTP + NH2NH2
ADP + phosphate + ?
-
-
-
-
?
ATP + UTP + NH2NH2
ADP + phosphate + CTP + N4-amino CTP
-
-
-
?
ATP + UTP + NH2OH
ADP + phosphate + N4-hydroxy-CTP
-
-
-
?
ATP + UTP + NH3
ADP + CTP + phosphate
ATP + UTP + NH3
ADP + phosphate + CTP
ATP + UTP + NH4+
ADP + phosphate + CTP
ATP + UTP + O-methylhydroxylamine
ADP + phosphate + N4-methoxyCTP
-
-
-
?
deoxyATP + UTP + NH4+
deoxyADP + phosphate + CTP
-
-
-
-
?
deoxyGTP + UTP + NH4+
deoxyGDP + phosphate + CTP
GTP + UTP + NH4+
GDP + phosphate + CTP
L-glutamine + H2O
L-glutamate + NH3
UTP + ATP + NH3
CTP + ADP + phosphate
additional information
?
-
ATP + dUTP + NH4+
ADP + phosphate + dCTP
-
half-saturating concentration of 0.6 mM for dUTP, it is unlikely that this reaction plays a significant physiological role
-
?
ATP + dUTP + NH4+
ADP + phosphate + dCTP
-
-
-
?
ATP + UTP + Gln
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + Gln
ADP + phosphate + CTP + Glu
-
-
-
?
ATP + UTP + Gln
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
-
-
-
?
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
-
-
-
?
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
-
-
-
-
?
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
-
-
-
?
ATP + UTP + Gln + H2O
ADP + CTP + Glu + phosphate
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
maximal activity with NH4+ is at least 20% greater than with glutamine
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
maximal activity with NH4+ is at least 20% greater than with glutamine
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + L-glutamate
-
the CTPS1-encoded enzyme is regulated by reversible phosphorylation at Thr455, regulation mechanisms, overview
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
-
?
ATP + UTP + glutamine
ADP + phosphate + CTP + L-glutamate
-
CTP synthetase is a cytosolic-associated glutamine amidotransferase enzyme that catalyzes the ATP-dependent transfer of the amide nitrogen from glutamine to the C-4 position of UTP to form CTP. CTP is an essential precursor of all membrane phospholipids that are synthesized via the Kennedy, i.e. CDP-choline and CDP-ethanolamine branches, and CDP-diacylglycerol pathways. The URA7-encoded CTP synthetase is responsible for the majority of the CTP made in vivo. Regulation mechanisms, detailed overview
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
CTPS catalyses the ATP-dependent formation of CTP from UTP using either ammonia or L-glutamine as the nitrogen source
-
-
?
ATP + UTP + L-glutamine
ADP + phosphate + CTP + L-glutamate
-
-
-
-
ir
ATP + UTP + NH3
ADP + CTP + phosphate
-
-
-
?
ATP + UTP + NH3
ADP + CTP + phosphate
-
-
-
?
ATP + UTP + NH3
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH3
ADP + phosphate + CTP
-
-
-
-
?
ATP + UTP + NH3
ADP + phosphate + CTP
CTPS catalyses the ATP-dependent formation of CTP from UTP using either ammonia or L-glutamine as the nitrogen source
-
-
?
ATP + UTP + NH3
ADP + phosphate + CTP
-
-
-
-
?
ATP + UTP + NH3
ADP + phosphate + CTP
-
CTPS1 is involved in microtubule network formation and/or stabilzation, overview
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
ir
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
last step in CTP biosynthesis
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
-
-
-
?
deoxyGTP + UTP + NH4+
deoxyGDP + phosphate + CTP
-
-
-
?
deoxyGTP + UTP + NH4+
deoxyGDP + phosphate + CTP
-
-
-
-
?
GTP + UTP + NH4+
GDP + phosphate + CTP
-
-
-
-
?
GTP + UTP + NH4+
GDP + phosphate + CTP
-
-
-
?
GTP + UTP + NH4+
GDP + phosphate + CTP
-
-
-
-
?
GTP + UTP + NH4+
GDP + phosphate + CTP
-
-
-
-
?
GTP + UTP + NH4+
GDP + phosphate + CTP
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
-
?
UTP + ATP + NH3
CTP + ADP + phosphate
-
the enzyme is regulated in a complex fashion, overview
-
-
?
UTP + ATP + NH3
CTP + ADP + phosphate
-
NH3 from glutamine deamination or exogenous
-
-
?
additional information
?
-
-
repression of the pyrG gene encoding cytidine triphosphate synthetase is responsive to cytidine nucleotide levels and is independent of both uridine nucleotides and PyrR-dependent attenuation
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
UTP- and CTP-binding structures, overview
-
-
?
additional information
?
-
-
UTP- and CTP-binding structures, overview
-
-
?
additional information
?
-
-
key enzyme for biosynthesis of cytosine ribonucleotides
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in synthesis of cytosine nucleotides from both de novo and uridine-salvage pathways
-
-
?
additional information
?
-
-
rate-limiting enzyme in the synthesis of cytosine nucleotides from both de novo and uridine-salvage pathways. In human lymphoblastic leukemia cells the synthesis of CTP occurs predominantly via CTP synthetase, whereas in proliferating normal human T lymphocytes the salvage of cytidine is preferred
-
-
?
additional information
?
-
-
the enzyme is one of the key enzymes in pyrimidine nucleotide anabolic pathways. The activity of this enzyme is elevated in various malignancies including acute lymphocytic leukemia
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
-
CTPS1 interacts with the GST-tagged peptidyl prolyl isomerase Pin1 from Xenopus laevis in a Ser575 phosphorylation-dependent manner, the CTPS1 also binds several other enzyme, e.g. alpha-tubulin, overview
-
-
?
additional information
?
-
-
CTP limitation increases expression of CTP synthase in Lactococcus lactis. At normal CTP concentrations a terminator is preferentially formed in the pyrG leader, thereby reducing expression of CTP synthase. At low CTP concentrations the RNA polymerase pauses at a stretch of C residues inthe pyrG leader, thereby allowing an antiterminator to form and transcription to proceed
-
-
?
additional information
?
-
-
in Lactococcus lactis the pyrG gene product is the only enzyme responsible for the amination of UTP to CTP
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
-
-
?
additional information
?
-
-
regulation of CTP synthetase activity by CTP plays an important role in the regulation of phospholipid synthesis
-
-
?
additional information
?
-
-
the enzyme is allosterically regulated by CTP product inhibition and by reversible phosphorylation
-
-
?
additional information
?
-
-
the enzyme can utilize NH3 as a substrate
-
-
?
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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'-deoxy-GTP
no guanosine, kact: 1.5/sec, KA: 0.21 mM, Ki: 0.36 mM; the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
2,6-diaminopurine riboside
-
2-Thiocytidine 5'-triphosphate
-
-
2-thiouridine 5'-triphosphate
-
-
3,7-dimethyluric acid
-
-
3-Deazauridine 5'-triphosphate
-
-
4-thiouridine 5'-triphosphate
-
-
6-diazo-5-oxo-L-norleucine
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
-
acivicin
-
irreversible inhibition by the glutamine analogue acivin. The acivicin inhibition of Trypanosoma brucei CTPS is more pronounced when the enzyme is preincubated with the drug in the presence of nucleotide substrates than in the absence of substrates
acycloguanosine monophosphate
-
adenosine 5'-[beta,gamma-imido]triphosphate
-
poor inhibitor compared to ATPgammaS
adenylyl-iminodiphosphate
-
competitive with ATP
alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
-
reduces the parasite CTP level even further and inhibits trypanosome proliferation in vitro and in Trypanosoma brucei-infected mice
Cu2+
-
inhibition is not reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM
cyclopentylcytosine triphosphate
-
-
D,L-2-amino-4-phosphonobutyrate
-
-
dCTP
-
very weak inhibitor
DELTA1-Pyrroline-5-carboxylate
-
weak
DL-DELTA1-pyrroline 5-carboxylate
-
0.125 mM, complete inhibition of ammonium chloride-dependent CTP synthesis
Gln
-
inhibition of hydroxylamine-dependent N4-OH CTP synthesis in presence of GTP
glutamate gamma-semialdehyde
-
potent linear mixed-type inhibitor, competitive with respect to ammonia, no inhibition of the mutant enzyme C379A
guanosine 5'-tetraphosphate
no guanosine, kact: 4/sec, KA: 0.19 mM, Ki: 0.5 mM; 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; the GTP analogue is capable of inhibiting Gln-dependent CTP formation at over 0.15 mM
L-2-pyrrolidone 5-carboxylate
-
weak competitive inhibition of the reaction with ammonia as substrate, no significant inhibition with glutamine as substrate
NH4Cl
-
substrate inhibition , a significant part of the inhibition can be shown to be due to the increase in ionic strength with increasing substrate concentrations
Ni2+
-
in presence of dithiothreitol inhibition at concentrations below 0.2 mM
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
p-chloromercuribenzenesulfonic acid
-
-
paraxanthine
-
pH-dependent inhibition, overview
PCMB
-
0.01 mM, 50% inhibition
pyrrole-2-carboxylate
-
weak competitive inhibition of the reaction with ammonia as substrate, no significant inhibition with glutamine as substrate
S-nitroso-L-cysteine
specific irreversible inhibitor,inhibits the activity by 94%
S-nitroso-L-homocysteine
specific irreversible inhibitor, inhibits the activity by 90%
theophylline
-
pH-dependent inhibition, overview
UTP
-
competitive with ATP
xanthine
-
pH-dependent inhibition, overview
Zn2+
-
inhibition is reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
reduces the parasite CTP level even further and inhibits trypanosome proliferation in vitro and in Trypanosoma brucei-infected mice
Caffeine
-
-
CTP
-
feedback inhibitor; IC50: 0.05 mM
CTP
-
cooperative inhibition
CTP
-
the enzyme from T lymphoblast S49 cells is refractory to complete inhibition by CTP
CTP
-
product inhibition of wild-type enzyme, mutant E161K is less sensitive to CTP product inhibition
CTP
-
IC50 for the native enzyme: 0.12 in presence of 0.5 mM ATP, 0.22 mM in presence of 1 mM ATP. IC50 for the phosphorylated enzyme: 0.21 mM in presence of 0.5 mM ATP, 0.31 mM in presence of 1 mM ATP
CTP
-
allosteric inhibition
CTP
-
allosteric regulation, product inhibition
cyclopentenyl cytosine
-
the inhibitor has a cytostatic effect on lymphoblasts of children with acute lymphocytic leukemia
cyclopentenyl cytosine
-
a highly specific inhibitor of CTPS1, in vivo inhibition leads to alterations in the cell nuclei and microtubule network, overview
GTP
-
inhibition of glutamine-dependent CTP formation above 0.15 mM, inhibition of glutamine-dependent CTP formation in a concentration-dependent manner
GTP
0.1 mM guanosine, kact: 10.3/sec, KA: 0.088 mM, Ki: 0.22 mM; 0.2 mM guanosine, kact: 8.2/sec, KA: 0.078 mM, Ki: 0.12 mM; 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; no guanosine, kact: 10.6/sec, KA: 0.081 mM, Ki: 0.28 mM
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
GTP
-
inhibition of N4-OH-CTP synthesis
GTP
-
inhibits glutamine-dependent CTP formation at concentrations above 0.2 mM
guanosine
-
uric acid
-
pH-dependent inhibition, overview
additional information
-
enzyme loses activity at ionic strengths higher than 0.4 M
-
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
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; 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.; no inhibition by S-nitrosoglutathione presumably due to its inability to enter the actve site of the enzyme
-
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
dithiothreitol
-
required for optimal activity, above 50 mM increase activity to 223% 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
2-mercaptoethanol
-
required for optimal activity, above 50 mM increase activity to 221%
2-mercaptoethanol
-
stimulates
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
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
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
GTP
-
allosteric activator
GTP
-
the binding of GTP to the allosteric site promotes coordination of the phosphorylation of UTP and hydrolysis of glutamine for optimal efficiency in CTP synthesis rather than just acting to increase the rate of glutamine hydrolysis itself
GTP
-
stimulates reaction with ATP, UTP and Gln
GTP
-
activates glutamine reaction, no activation of ammonia reaction
GTP
-
essential activator when glutamine is the nitrogen source
GTP
-
not essential, but acts as activator on the glutamine reaction, optimal activation at 1 mM
GTP
-
activates glutamine-dependent CTP formation at concentrations below 0.2 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
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
-
additional information
-
the URA7-encoded enzyme is phosphorylated by protein kinases A and C at Ser424, and these phosphorylations stimulate CTP synthetase activity and increase cellular CTP levels and the utilization of the Kennedy pathway
-
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0.0058 - 0.054
2',3'-dialdehyde adenosine 5'-triphosphate
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
additional information
additional information
-
-
-
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
1.86
Gln
37°C, 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
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
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
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
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
37°C, 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
10.1
NH3
37°C, pH 8.0, mutant enzyme L109A
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
1.8
NH4+
-
30°C, pH 8.0, mutant enzyme G360P
5.1
NH4+
-
30°C, pH 8.0, mutant enzyme R359P
6.3
NH4+
-
30°C, pH 8.0, wild-type enzyme
6.9
NH4+
-
30°C, pH 8.0, mutant enzyme R359M
7.5
NH4+
-
30°C, pH 8.0, mutant enzyme G360A
10.1
NH4+
-
30°C, pH 8.0, mutant enzyme E362Q
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
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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0.079 - 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
0.33 - 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
0.063 - 0.09
3,7-dimethyluric acid
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
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
-
0.079
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
0.33
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
0.063
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
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
12.9
adenine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
15.8
adenine
Escherichia coli
-
pH 8.0, Gln-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
0.39
Caffeine
Escherichia coli
-
pH 8.0, Gln-dependent CTP formation
0.48
Caffeine
Trypanosoma brucei
-
in HEPES buffer (70 mM, pH 7.3), at 37°C
0.51
Caffeine
Escherichia coli
-
pH 8.0, NH3-dependent CTP formation
0.04
CTP
Homo sapiens
wild-type, pH 8.1, 37°C
0.042
CTP
Homo sapiens
wild-type, pH 8.1, 37°C
0.045
CTP
Homo sapiens
mutant S571A, pH 8.1, 37°C
0.05
CTP
Chlamydia trachomatis
-
IC50: 0.05 mM
0.057
CTP
Homo sapiens
C-terminal deletion mutant, pH 8.1, 37°C
0.072
CTP
Homo sapiens
mutant S568A, pH 8.1, 37°C
0.15
CTP
Escherichia coli
-
IC50: 0.15 mM
0.21
CTP
Saccharomyces cerevisiae
-
IC50 for the native enzyme: 0.12 in presence of 0.5 mM ATP, 0.22 mM in presence of 1 mM ATP. IC50 for the phosphorylated enzyme: 0.21 mM in presence of 0.5 mM ATP, 0.31 mM in presence of 1 mM ATP
0.3
CTP
Saccharomyces cerevisiae
-
IC50: 0.3 mM
0.32
CTP
Saccharomyces cerevisiae
-
IC50: 0.32 mM
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
0.46
GTP
Trypanosoma brucei
-
in HEPES buffer (70 mM, pH 7.3), at 37°C
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
0.38
guanosine
Trypanosoma brucei
-
in HEPES buffer (70 mM, pH 7.3), at 37°C
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
0.44
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
0.1
uric acid
Trypanosoma brucei
-
in HEPES buffer (70 mM, pH 7.3), at 37°C
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
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
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A20R
mutation disrupts cytoophidium assembly
DELTA20
deletion of the N-terminal 20 amino acids alone is sufficient to disrupt cytoophidium assembly, mutant protein forms distinct cytoplasmic structures which appear as large clusters
K2E
mutation disrupts cytoophidium assembly
Y3E
mutation disrupts cytoophidium assembly
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
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
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
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
E579A
HEK 293 cells: no effect on phosphorylation of CTPS1 by glycogen synthase kinase 3
S462A/T455A
-
S462A and T455A mutations result in a decreased CTP synthetase 1 phosphorylation which appear to be much less than of the individual mutant enzymes S462A or T455A
S568A
2fold increase in Km value for UTP. Mutation of S568A significantly increases CTPS2 activity. The S568A mutation has a greater effect on the glutamine than ammonia-dependent activity
S571A
4fold increase in Km value for UTP
S571I
Ser-571 is the major site phosphorylated by glycogen synthase kinase 3 in intact human embryonic kidney 293 cells
S571I/S574A
phosphorylation by glycogen synthase kinase 3 does not show altered incorporation of phosphate compared with S571I alone
S571I/S574A/S575A
phosphorylation by glycogen synthase kinase 3 shows a slight decrease in the amount of phosphate incorporated into CTPS1 compared with S571I/S575A, suggesting that Ser-574 may serve as a minor secondary site for glycogen synthase kinase 3 phosphorylation
S571I/S575A
phosphorylation by glycogen synthase kinase 3 shows slightly elevated amounts of phosphate incorporated into CTPS1 compared with S571I, suggesting that without the ability to phosphorylate Ser-571 or Ser-575 in vitro, glycogen synthase kinase 3 may phosphorylate an alternative site, albeit to a much lesser extent
S574A
greatly reduces phosphorylation by glycogen synthase kinase 3
S574A/S575A
greatly reduces phosphorylation by glycogen synthase kinase 3
T455A
-
T455A mutation causes a 78% decrease in protein kinase A phosphorylation
E362Q
-
turnover number for NH4Cl-dependent GTP synthesis reaction is 1.6fold higher than wild-type value
G360A
-
5fold increase in GTP-dependent activation of uncoupled glutamine hydrolysis compared to wild-type enzyme. Turnover number for NH4Cl-dependent GTP synthesis reaction is 1.2fold higher than wild-type value
G360P
-
mutant enzyme shows no GTP activation of the uncoupled glutaminase reaction, about 4fold lower turnover number for NH4Cl-dependent CTP synthesis reaction than wild-type enzyme
R359M
-
mutant enzyme shows no GTP activation of the uncoupled glutaminase reaction. Turnover number for NH4Cl-dependent GTP synthesis reaction is 1.1fold higher than wild-type value
R359P
-
mutant enzyme shows no GTP activation of the uncoupled glutaminase reaction. Turnover number for NH4Cl-dependent GTP synthesis reaction is 1.2fold lower than wild-type value
D70A
mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments
E146A
mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments
R381M
mutation in L11 lid, 3.1fold increase in the number of cells forming filaments
R381P
mutation in L11 lid, 3.1fold increase in the number of cells forming filaments
S330A
-
CTP synthetase activity in cells bearing the mutant enzyme is elevated, mutation causes an elevation in the Vmax of the reaction. Mutation does not have a major effect on the oligomerization of CTP synthetase
S354A
-
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 98% greater compared to wild-type enzyme
S454A
-
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme. Mutation does not have a major effect on the oligomerization of CTP synthetase
D70A
-
mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments
-
E146A
-
mutation in the ATP binding site, mutant exhibits approximately twofold increase in the number of cells containing filaments
-
E161K
-
mutation in CTP binding site, filament formation is completely disrupted and the enzyme can only form foci. Mutation decreases the affinity of the enzyme for CTP
-
S36A
-
mutation in phosphorylation site, causes an approximately twofold decrease in the frequency of filament formation
-
D149E
-
the single point mutation in the resistant strain L2/CPEC results in loss of CTP feedback inhibition, cells are resistant to the cytotoxic effects of cyclopentenyl cytosine
D149E
-
the single point mutation in the resistant strain L2/CPEC results in loss of CTP feedback inhibition, cells are resistant to the cytotoxic effects of cyclopentenyl cytosine
-
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
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
S575A
greatly reduces phosphorylation by glycogen synthase kinase 3. Mutation of Ser-575 prevents the phosphorylation of Ser-571, suggesting that phosphorylation of Ser-575 is necessary for priming the glycogen synthase kinase 3 phosphorylation of Ser-571
S575A
-
site-directed mutagenesis the mutant does not interact with peptidyl prolyl isomerase Pin1
E161K
-
specific activity of the mutant URA7-encoded and URA8-encoded enzymes are 2fold greater when compared with the wild-type enzymes. The mutant enzymes are less sensitive to CTP product inhibition with inhibitor constants for CTP of 8.4fold- and 5.5fold greater, respectively, than those of their wild-type counterparts. Cells expressing the E161K mutant enzymes on a multicopy plasmid exhibit an increase in resistance to the pyrimidine poison and cancer therapeutic drug cyclopentenylcytosine and accumulate elevated levels of CTP when compared with cells expressing the wild-type enzymes. Cells expressing the E161K mutation in the URA7-encoded CTP synthetase exhibit an 1.5fold increase in the utilization of the Kennedy pathway for phosphatidylcholine synthesis when compared with control cells. Cells bearing the mutation also exhibit an 1.5fold increase in the synthesis of phosphatidylcholine, 1.3fold for phosphatidylethanolamine and 2fold for phosphatidate and a 1.7fold decrease in synthesis of phosphatidylserine. Cells bearing the e161K mutation exhibit an 1.6fold increase in the ratio of total neutral lipids to phospholipids, an 1.4fold increase in triacylglycerol, a 1.7fold increase in free fatty acids, an1.8fold increase in ergosterol ester and a 1.3fold decrease in diacylgylcerol when compared with control cells
E161K
mutation in CTP binding site, filament formation is completely disrupted and the enzyme can only form foci. Mutation decreases the affinity of the enzyme for CTP
S36A
-
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 54% greater compared to wild-type enzyme
S36A
mutation in phosphorylation site, causes an approximately twofold decrease in the frequency of filament formation
additional information
in cytoophidium assembly, formation of heteromeric CTP synthase filaments takes place, which is disrupted by CTP synthase carrying a mutated N-terminal alanine residue. N-terminal swapping, i.e. exchange of the 20 N-terminal amino acids to the residues of human and yeast CTP synthase does not affect CTPsyn cytoophidium assembly
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
additional information
-
deletion of the C-terminal regulatory domain, residues Ser562-Asp591, of CTPS1 greatly increases the Vmax of the enzyme
additional information
deletion of the C-terminal regulatory domain, residues Ser562-Asp591, of CTPS1 greatly increases the Vmax of the enzyme
additional information
-
the ura7D/ura8D double mutant, that lacks CTP synthetase activity, shows a lethal phenotype, which can be rescued by functional expression of human CTPS1 and CTPS2 genes that encode CTP synthetase enzymes. In an ura8 mutant, CTP levels are 22% lower than in wild-type, whereas the CTP concentration in an ura7 mutant is 64% lower than in wild-type
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Saccharomyces cerevisiae (P28274), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P28274)
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