6.3.4.2	additional information	-	-	690817	
6.3.4.2	additional information	-	a structure-activity study using a variety of GTP and guanosine analogues reveals that only a few GTP analogues are capable of activating Gln-dependent CTP formation to varying degrees: GTP > 6-thio-GTP > ITP> guanosine 5'-tetraphosphate > O-methyl-GTP > 2'-deoxy-GTP. No activation is observed with guanosine, GMP, GDP, 2',3'-dideoxy-GTP, acycloguanosine, and acycloguanosine monophosphate indicating that the 5'-triphosphate, 2'-OH, and 3'-OH are required for full activation. The 2-NH2 group is important in binding recognition while substituents at the 6-position are important in activation.	674909	
6.3.4.2	additional information	-	CTP synthetase 1 activity of the T455A mutant enzyme is 2fold higher than the wild type enzyme. T455A mutation causes a 44% decrease in the amount of human CTP synthetase 1 that is phosphorylated in Saccharomyces cerevisiae cells, accompanied by a 2.5fold increase in the cellular concentration of CTP and a 1.5-fold increase in the choline-dependent synthesis of phosphatidylcholine	674886	
6.3.4.2	additional information	-	during the purification, the specific activity of the enzyme preparation increased 836fold and the total yield is 28%	674786	
6.3.4.2	additional information	-	fast assay allows the processing of a large number of samples	648996	
6.3.4.2	additional information	-	low serum is found to decrease CTPS1 activity, and incubation with the glycogen synthase kinase 3 inhibitor indirubin-3’-monoxime protects against this decrease in activity. Incubation with an alkaline phosphatase increases CTPS1 activity in a time-dependent manner, demonstrating that phosphorylation inhibits CTPS1 activity	674862	
6.3.4.2	additional information	-	S462A mutation results in 61%-reduced CTP synthetase 1 phosphorylation. The Saccharomyces cerevisiae-expressed and purified S462A mutant enzyme exhibits a 2fold reduction in CTP synthetase 1 activity, whereas the purified T455A mutant enzyme exhibited a 2fold elevation in CTP synthetase 1 activity, implying that that protein kinase C phosphorylation at Ser462 stimulates human CTP synthetase 1 activity, whereas phosphorylation at Thr455 inhibits activity	674816	
6.3.4.2	additional information	-	T455A mutation results in 58%-reduced CTP synthetase 1 phosphorylation. The Saccharomyces cerevisiae-expressed and purified S462A mutant enzyme exhibits a 2fold reduction in CTP synthetase 1 activity, whereas the purified T455A mutant enzyme exhibited a 2fold elevation in CTP synthetase 1 activity, implying that that protein kinase C phosphorylation at Ser462 stimulates human CTP synthetase 1 activity, whereas phosphorylation at Thr455 inhibits activity	674816	
6.3.4.2	additional information	-	Thr 455 is identified as a major site of phosphorylation by protein kinase A, phosphorylation at Thr455 results in the inhibition of activity in vitro and in vivo. Data indicate that phosphorylation at Thr455 attenuates the choline-dependent synthesis of phosphatidylcholine when CTP synthetase 1 enzyme is expressed in Saccharomyces cerevisiae	674886	
6.3.4.2	0.00066	-	crude extract of protein	674786	
6.3.4.2	0.0025	-	specific activity of Escherichia coli expressed enzyme, after a 20 min incubation with protein kinase C, the activity of the CTP synthetase was stimulated 95fold	674816	
6.3.4.2	0.015	-	-	648988, 648991	
6.3.4.2	0.06	-	-	648987	
6.3.4.2	0.1119	-	1st Talon eluate	674786	
6.3.4.2	0.2	-	mutant enzyme S354A	648973	
6.3.4.2	0.3	-	mutant enzyme S36A	648973	
6.3.4.2	0.3986	-	TEV-cleaved 2nd Talon flow-through	674786	
6.3.4.2	0.5515	-	concentrated SourceQ flow-through	674786	
6.3.4.2	0.6	-	mutant enzyme S454A	648973	
6.3.4.2	0.66	-	wild-type enzyme	648973	
6.3.4.2	0.83	-	mutant enzyme S330A	648973	
6.3.4.2	1.3	-	-	648978	
6.3.4.2	2.51	-	-	648999	
6.3.4.2	5.8	6.1	-	648981, 648989, 648992	
6.3.4.2	8.7	-	-	648984