6.3.4.2	?	x * 100000, SDS-PAGE	662806	
6.3.4.2	?	x * 56180, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 59500, calculated	-, 746547	
6.3.4.2	?	x * 64622, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 64783, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 65514, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 65678, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 66705,calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 66710, calculation from nucleotide sequence	648966	
6.3.4.2	?	x * 70000, SDS-PAGE	727139, 727427, 728541	
6.3.4.2	dimer	2 * 66000, SDS-PAGE	648982	
6.3.4.2	dimer	crystallization data and sedimentation-ultracentrifugation experiments	713658	
6.3.4.2	dimer	the enzyme is a dimer of 108000 Da, the dimer associates to form a tetramer in the presence of either ATP or UTP	-, 648981	
6.3.4.2	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	690817	
6.3.4.2	additional information	CTP synthetase oligomerizes to a tetramer in the presence of its substrates UTP and ATP	648999	
6.3.4.2	additional information	the enzyme can dissociate to an apparently inactive monomer. The dissociation is reversible and the rate of association is slow	648984	
6.3.4.2	tetramer	-	648968	
6.3.4.2	tetramer	2 * 60000	648977	
6.3.4.2	tetramer	4 * 50000, SDS-PAGE	648984	
6.3.4.2	tetramer	4 * 52000, enzyme exists as tetramer in presence of UTP, Mg2+ and ATP	648989, 648992	
6.3.4.2	tetramer	4 * 68000, SDS-PAGE	648999	
6.3.4.2	tetramer	conserved Gly142 is critical for tetramerization, overview	690817	
6.3.4.2	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	648975	
6.3.4.2	tetramer	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	648978