Carbamoyl phosphate synthetase (glutamine-hydrolyzing): increased activity in cancer cells.
The specific activity of carbamoyl phosphate synthetase (glutamine-hydrolyzing), the first and rate-limiting enzyme of de novo uridine 5'-triphosphate biosynthesis, was increased in 13 transplantable hepatomas, particularly in the rapidly growing tumors (5.7- to 9.5-fold), and the rise was correlated with tumor growth rates. Thus, synthetase activity was linked with both hepatic neoplastic transformation and progression. Synthetase specific activity was so elevated in a transplantable sarcoma (18-fold) and a kidney adenocarcinoma (5-fold). The increased activity should enhance the capacity of the pathway and should confer selective advantages to cancer cells.
D000230:Adenocarcinoma / Q000201:enzymology; D000818:Animals; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) / Q000378:metabolism*; D002454:Cell Differentiation; D007680:Kidney Neoplasms; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008114:Liver Neoplasms, Experimental / Q000201:enzymology* / Q000473:pathology; D008115:Liver Regeneration; D009368:Neoplasm Transplantation; D051381:Rats; D012513:Sarcoma, Experimental / Q000201:enzymology
D008025:Ligases; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)