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EC Tree
IUBMB Comments The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP [4,5]. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution [3,6].
The taxonomic range for the selected organisms is: Mus musculus The enzyme appears in selected viruses and cellular organisms
Synonyms
ctps, ctp synthetase, ctp synthase, ctps1, ctpsyn, ctps2, cytidine triphosphate synthetase, ctp synthetase 1, cytidine 5'-triphosphate synthase, ecctps,
more
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cytidine 5'-triphosphate synthetase
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cytidine triphosphate synthetase
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synthetase, cytidine triphosphate
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uridine triphosphate aminase
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-
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UTP-ammonia ligase
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-
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CTPS
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-
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UTP:ammonia ligase (ADP-forming)
The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP [4,5]. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution [3,6].
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ATP + UTP + NH4+
ADP + phosphate + CTP
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-
?
ATP + UTP + CH3NHOH
ADP + phosphate + ?
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-
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?
ATP + UTP + glutamine
ADP + phosphate + CTP + Glu
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-
-
-
?
ATP + UTP + hydroxylamine
ADP + phosphate + N4-hydroxyCTP
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activity is about 3fold higher than activity with NH4+
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?
ATP + UTP + NH2NH2
ADP + phosphate + ?
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
ATP + UTP + O-methylhydroxylamine
ADP + phosphate + N4-methoxyCTP
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-
-
?
deoxyATP + UTP + NH4+
deoxyADP + phosphate + CTP
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?
deoxyGTP + UTP + NH4+
deoxyGDP + phosphate + CTP
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?
GTP + UTP + NH4+
GDP + phosphate + CTP
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-
-
?
additional information
?
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ATP + UTP + NH4+
ADP + phosphate + CTP
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
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-
-
?
ATP + UTP + NH4+
ADP + phosphate + CTP
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?
ATP + UTP + NH4+
ADP + phosphate + CTP
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?
additional information
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
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additional information
?
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additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
additional information
?
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CTP synthetase plays a pivotal role in the synthesis of CTP and dCTP
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?
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Mg2+
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absolutely dependent on
Mg2+
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absolute requirement
Mg2+
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required, no activity in absence of
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adenylyl-iminodiphosphate
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competitive with ATP
cyclopentylcytosine triphosphate
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PCMB
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0.01 mM, 50% inhibition
UTP
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competitive with ATP
CTP
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mixed inhibition
CTP
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the enzyme from T lymphoblast S49 cells is refractory to complete inhibition by CTP
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2-mercaptoethanol
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required for optimal activity, above 50 mM increase activity to 221%
dithiothreitol
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required for optimal activity, above 50 mM increase activity to 223% mM
GTP
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activates glutamine reaction, no activation of ammonia reaction
GTP
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essential activator when glutamine is the nitrogen source
GTP
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not essential, but acts as activator on the glutamine reaction, optimal activation at 1 mM
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1.1
adenylyliminodiphosphate
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pH 8.6
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8.6
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reaction with ammonia
8.6 - 8.9
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reaction with glutamine
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7.3 - 9.5
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pH 7.3: about 35% of maximal activity, pH 9.5: about 40% of maximal activity
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CTP synthetase type II
SwissProt
brenda
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brenda
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brenda
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embryonic brain
brenda
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brenda
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embryonic brain
brenda
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brenda
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brenda
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brenda
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brenda
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physiological function
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CTP synthase protein molecules form filamentous structures termed cytoophidia or CTP synthase filaments in the cytoplasm and nucleus
physiological function
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overexpression of CTPS by in utero electroporation in the embryonic mouse brain induces formation of cytoophidia in developing cortical neurons and impairs neuronal migration. The increase of cytoophidia accelerates neuronal differentiation and inhibits neural progenitor cell proliferation by reducing their mitotic activity. The cytoophidia diffuse during the early G1-phase of the cell cycle
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PYRG1_MOUSE
591
0
66682
Swiss-Prot
other Location (Reliability: 3 )
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66710
x * 66710, calculation from nucleotide sequence
122000
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sucrose density gradient centrifugation
65514
x * 65514, calculation from nucleotide sequence
66000
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2 * 66000, SDS-PAGE
70000
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x * 70000, SDS-PAGE
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?
x * 66710, calculation from nucleotide sequence
dimer
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2 * 66000, SDS-PAGE
?
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x * 70000, SDS-PAGE
?
x * 65514, calculation from nucleotide sequence
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2-mercaptoethanol is required for optimal stabilization of enzyme activity
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-20°C, 30% glycerol, 100 mM 2-mercaptoethanol, 40% loss of activity after 4 weeks
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-80°C, 30% glycerol, 100 mM 2-mercaptoethanol, 65% of the original activity is retained after 4 weeks
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4°C, 30% glycerol, 100 mM 2-mercaptoethanol, 65% loss of activity after 4 weeks
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Ni2+-IDA resin column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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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
Kizaki, H.; Ohsaka, F.; Sakurada, T.
CTP synthetase from Ehrlich ascites tumor cells. Subunit stoichiometry and regulation of activity
Biochim. Biophys. Acta
829
34-43
1985
Mus musculus
brenda
Kizaki, H.; Ohsaka, F.; Sakurada, T.
Role of GTP in CTP synthetase from Ehrlich ascites tumor cells
Biochem. Biophys. Res. Commun.
108
286-291
1982
Mus musculus
brenda
Kizaki, H.; Sakurada, T.; Weber, G.
Purification and properties of CTP synthetase from Ehrlich ascites tumor cells
Biochim. Biophys. Acta
662
48-54
1981
Mus musculus
brenda
Kang, G.J.; Cooney, D.A.; Moyer, J.D.; Kelley, J.A.; Kim, H.Y.; Marquez, V.E.; Johns, D.G.
Cyclopentenylcytosine triphosphate. Formation and inhibition of CTP synthetase
J. Biol. Chem.
264
713-718
1989
Mus musculus
brenda
Aronow, B.; Ullman, B.
In situ regulation of mammalian CTP synthetase by allosteric inhibition
J. Biol. Chem.
262
5106-5112
1987
Mus musculus
brenda
Kizaki, H.; Ohsaka, F.; Sakurada, T.
Synthesis of N4-substituted CTP by mammalian CTP synthetase
Biochem. Biophys. Res. Commun.
145
569-574
1987
Mus musculus
brenda
Gou, K.M.; Chang, C.C.; Shen, Q.J.; Sung, L.Y.; Liu, J.L.
CTP synthase forms cytoophidia in the cytoplasm and nucleus
Exp. Cell Res.
323
242-253
2014
Homo sapiens, Mus musculus
brenda
Li, X.; Xie, J.; Hei, M.; Tang, J.; Wang, Y.; Foerster, E.; Zhao, S.
High level of CTP synthase induces formation of cytoophidia in cortical neurons and impairs corticogenesis
Histochem. Cell Biol.
149
61-73
2018
Mus musculus
brenda