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Results 1 - 10 of 23 > >>
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Reference
-999
-
-
-999
-
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.
-999
-
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; 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
-999
-
during the purification, the specific activity of the enzyme preparation increased 836fold and the total yield is 28%
-999
-
fast assay allows the processing of a large number of samples
-999
-
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
-999
-
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; 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
0.00066
-
crude extract of protein
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
Results 1 - 10 of 23 > >>