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Literature summary for 6.3.4.2 extracted from

  • Pappas, A.; Yang, W.L.; Park, T.S.; Carman, G.M.
    Nucleotide-dependent tetramerization of CTP synthetase from Saccharomyces cerevisiae (1998), J. Biol. Chem., 273, 15954-15960.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of the purified native CTP synthetase with protein kinase A and protein kinase C facilitates the nucleotide-dependent tetramerization. Dephosphorylation of native CTP-desynthetase with alkaline phosphatase prevents the nucleotide-dependent tetramerization of the enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + NH4+
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Saccharomyces cerevisiae ADP + phosphate + CTP
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Subunits

Subunits Comment Organism
tetramer 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 Saccharomyces cerevisiae