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)
ECTree
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General Information
General Information on EC 6.3.4.2 - CTP synthase (glutamine hydrolysing)
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malfunction
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mutations disrupting CTP synthase isoform C or isoform A expression results in cytoophidium disassembly
physiological function
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central role of CTP in the biosynthesis of nucleic acids, phospholipids, and sialic acid
physiological function
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CTP synthase forms filaments in Caulobacter crescentus, and the filaments it forms regulate the curvature of Caulobacter crescentus cells independently of its catalytic function. The morphogenic role of CTP synthase requires its functional interaction with the intermediate filament, crescentin
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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CTP synthase protein molecules form filamentous structures termed cytoophidia or CTP synthase filaments in the cytoplasm and nucleus
physiological function
destabilization of the active tetrameric form of the enzyme increases filament formation. The sites responsible for feedback inhibition and allosteric activation control filament length, implying that multiple regions of the enzyme can influence filament structure. Blocking catalysis without disrupting the regulatory sites of the enzyme does not affect filament formation or length
physiological function
in cytoophidium assembly, formation of heteromeric CTP synthase filaments takes place, which is disrupted by CTP synthase carrying a mutated N-terminal alanine residue
physiological function
in ovarian germline cells CTPS filaments are catalytically active and their assembly is regulated by the non-receptor tyrosine kinase DAck. Egg chambers from flies deficient in DAck catalytic activity exhibit disrupted CTPS filament architecture and morphological defects that correlate with reduced fertility. Ovaries from these flies exhibit reduced levels of total RNA
physiological function
Myc protein levels correlate with cytoophidium abundance in follicle epithelia. Reducing Myc levels results in cytoophidium loss and small nuclear size in follicle cells, while overexpression of Myc increases the length of cytoophidia and the nuclear size of follicle cells. Ectopic expression of Myc induces cytoophidium formation in late stage follicle cells. Furthermore, knock-down of CTPsyn is sufficient to suppress the overgrowth phenotype induced by Myc overexpression
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
physiological function
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destabilization of the active tetrameric form of the enzyme increases filament formation. The sites responsible for feedback inhibition and allosteric activation control filament length, implying that multiple regions of the enzyme can influence filament structure. Blocking catalysis without disrupting the regulatory sites of the enzyme does not affect filament formation or length
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