This article will address the issue of Carbamoyl phosphate synthase II, an issue of great relevance today. Carbamoyl phosphate synthase II has captured the attention of experts and the general public, generating a wide debate in various areas. Over the years, Carbamoyl phosphate synthase II has been the subject of extensive research and has undergone significant changes, prompting increased interest in understanding its impact and scope. In this context, it is essential to analyze in detail the implications of Carbamoyl phosphate synthase II and its influence in different contexts. This article will seek to exhaustively explore the different facets of Carbamoyl phosphate synthase II, delving into its most relevant aspects and providing a comprehensive view of its importance in the current panorama.
Carbamoyl phosphate synthetase (glutamine-hydrolysing) (EC6.3.5.5) is an enzyme that catalyzes the reactions that produce carbamoyl phosphate in the cytosol (as opposed to type I, which functions in the mitochondria). Its systemic name is hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating).[1][2][3][4][5][6][7][8]
In pyrimidine biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:
It is activated by ATP and PRPP[9] and it is inhibited by UTP (Uridine triphosphate)[10]
Neither CPSI nor CPSII require biotin as a coenzyme, as seen with most carboxylation reactions.
It is one of the four functional enzymatic domains coded by the CAD gene.[11] The CAD gene is a large gene. It uses a single strand to code for these enzyme jobs. It is classified under EC6.3.5.5.
^Anderson PM, Meister A (December 1965). "Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase". Biochemistry. 4 (12): 2803–9. doi:10.1021/bi00888a034. PMID5326356.
^Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL, Mullins LS, Raushel FM (November 1996). "Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase". Biochemistry. 35 (45): 14352–61. doi:10.1021/bi961183y. PMID8916922.
^Holden HM, Thoden JB, Raushel FM (December 1998). "Carbamoyl phosphate synthetase: a tunnel runs through it". Current Opinion in Structural Biology. 8 (6): 679–85. doi:10.1016/s0959-440x(98)80086-9. PMID9914247.
^Raushel FM, Thoden JB, Reinhart GD, Holden HM (October 1998). "Carbamoyl phosphate synthetase: a crooked path from substrates to products". Current Opinion in Chemical Biology. 2 (5): 624–32. doi:10.1016/s1367-5931(98)80094-x. PMID9818189.
^Raushel FM, Thoden JB, Holden HM (June 1999). "The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia". Biochemistry. 38 (25): 7891–9. doi:10.1021/bi990871p. PMID10387030.