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Information on EC 6.3.4.2 - CTP synthase (glutamine hydrolysing) and Organism(s) Mus musculus and UniProt Accession P70303
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6.3.4.2 CTP synthase (glutamine hydrolysing)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].
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- 6.3.4.2
- pyrimidine
- cytosine
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cytoophidia
- dctp
-
cyclopentenyl
- deoxycytidine
- acivicin
-
glutamine-dependent
- 3-deazauridine
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rheumatology
- l-glutamine
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alliance
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carra
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ctpas
- pyrazofurin
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uridine-cytidine
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rheumatologist
- 6-diazo-5-oxo-l-norleucine
- drug development
- medicine
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTP synthetase
-
-
-
-
CTPS
cytidine 5'-triphosphate synthetase
-
-
-
-
cytidine triphosphate synthetase
-
-
-
-
synthetase, cytidine triphosphate
-
-
-
-
uridine triphosphate aminase
-
-
-
-
UTP-ammonia ligase
-
-
-
-
CTPS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY
9023-56-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + UTP + hydroxylamine
ADP + phosphate + N4-hydroxyCTP
-
activity is about 3fold higher than activity with NH4+
-
?
ATP + UTP + O-methylhydroxylamine
ADP + phosphate + N4-methoxyCTP
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CTP
-
the enzyme from T lymphoblast S49 cells is refractory to complete inhibition by CTP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
required for optimal activity, above 50 mM increase activity to 221%
dithiothreitol
-
required for optimal activity, above 50 mM increase activity to 223% mM
GTP
-
not essential, but acts as activator on the glutamine reaction, optimal activation at 1 mM
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3 - 9.5
-
pH 7.3: about 35% of maximal activity, pH 9.5: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
CTP synthase protein molecules form filamentous structures termed cytoophidia or CTP synthase filaments in the cytoplasm and nucleus
physiological function
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PYRG2_MOUSE
586
0
65514
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30% glycerol, 100 mM 2-mercaptoethanol, 40% loss of activity after 4 weeks
-
-80°C, 30% glycerol, 100 mM 2-mercaptoethanol, 65% of the original activity is retained after 4 weeks
-
4°C, 30% glycerol, 100 mM 2-mercaptoethanol, 65% loss of activity after 4 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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
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
Aronow, B.; Ullman, B.
In situ regulation of mammalian CTP synthetase by allosteric inhibition
J. Biol. Chem.
262
5106-5112
1987
Mus musculus
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
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
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