6.3.4.2: CTP synthase (glutamine hydrolysing)
This is an abbreviated version!
For detailed information about CTP synthase (glutamine hydrolysing), go to the full flat file.
Word Map on EC 6.3.4.2
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6.3.4.2
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pyrimidine
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cytosine
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cytoophidia
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dctp
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cyclopentenyl
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deoxycytidine
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acivicin
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glutamine-dependent
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3-deazauridine
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rheumatology
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l-glutamine
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alliance
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carra
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ctpas
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pyrazofurin
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uridine-cytidine
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rheumatologist
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6-diazo-5-oxo-l-norleucine
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drug development
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medicine
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analysis
- 6.3.4.2
- pyrimidine
- cytosine
-
cytoophidia
- dctp
-
cyclopentenyl
- deoxycytidine
- acivicin
-
glutamine-dependent
- 3-deazauridine
-
rheumatology
- l-glutamine
-
alliance
-
carra
-
ctpas
- pyrazofurin
-
uridine-cytidine
-
rheumatologist
- 6-diazo-5-oxo-l-norleucine
- drug development
- medicine
- analysis
Reaction
Synonyms
CTP synthase, CTP synthase 1, CTP synthetase, CTP synthetase 1, CTPS, CTPS1, CTPS2, CTPsyn, CTS, cytidine 5'-triphosphate synthase, cytidine 5'-triphosphate synthetase, cytidine triphosphate synthetase, cytidine triphosphate synthetase 1, EcCTPS, pfCTP synthetase, PyrG, synthetase, cytidine triphosphate, URA7, uridine triphosphate aminase, UTP-ammonia ligase, UTP:ammonia ligase (ADP-forming)
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Subunits
Subunits on EC 6.3.4.2 - CTP synthase (glutamine hydrolysing)
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dimer
tetramer
additional information
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the enzyme is a dimer of 108000 Da, the dimer associates to form a tetramer in the presence of either ATP or UTP
dimer
Escherichia coli B / ATCC 11303
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the enzyme is a dimer of 108000 Da, the dimer associates to form a tetramer in the presence of either ATP or UTP
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dimer
crystallization data and sedimentation-ultracentrifugation experiments
tetramer
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4 * 52000, enzyme exists as tetramer in presence of UTP, Mg2+ and ATP
tetramer
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UTP and ATP are responsible for the tetramerization and activation of the inactive dimeric form of the enzyme. UTP is absolutely required for the tatramerization of the enzyme when ATP is present at a saturating concentration
tetramer
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the enzyme exists as an inactive dimer in the absence of ATP and UTP. In the presence of saturating concentrations of ATP and UTP, the CTP synthetase protein exists as an active tetramer. Increasing concentrations of ATP and UTP cause a dose-dependent conversion of the dimeric species to a tetramer. Tetramerization is dependent on UTP and Mg2+ ions. ATP facilitates the UTP-dependent teramerization of CTP synthetase by a mechanism that involves the ATP-dependent phosphorylation of UTP catalyzed by the enzyme
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the enzyme can dissociate to an apparently inactive monomer. The dissociation is reversible and the rate of association is slow
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. Oligomerization of Gly mutant enzymes, overview
additional information
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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. Oligomerization of Gly mutant enzymes, overview
additional information
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CTP synthetase oligomerizes to a tetramer in the presence of its substrates UTP and ATP