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Carbamoyl phosphate synthase II
Class of enzymes

Carbamoyl phosphate synthetase (glutamine-hydrolysing) (EC 6.3.5.5) 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).

In pyrimidine biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:

2 ATP + L-glutamine + HCO3− + H2O ⇌ {\displaystyle \rightleftharpoons } 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction) (1a) L-glutamine + H2O ⇌ {\displaystyle \rightleftharpoons } L-glutamate + NH3 (1b) 2 ATP + HCO3− + NH3 ⇌ {\displaystyle \rightleftharpoons } 2 ADP + phosphate + carbamoyl phosphate

It is activated by ATP and PRPP and it is inhibited by UTP (Uridine triphosphate) 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. The CAD gene is a large gene. It uses a single strand to code for these enzyme jobs. It is classified under EC 6.3.5.5.

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See also

References

  1. 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. PMID 5326356. /wiki/Doi_(identifier) ↩

  2. Kalman SM, Duffield PH, Brzozowski T (April 1966). "Purification and properties of a bacterial carbamyl phosphate synthetase". The Journal of Biological Chemistry. 241 (8): 1871–7. doi:10.1016/S0021-9258(18)96716-5. PMID 5329589. https://doi.org/10.1016%2FS0021-9258%2818%2996716-5 ↩

  3. Yip MC, Knox WE (May 1970). "Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues". The Journal of Biological Chemistry. 245 (9): 2199–204. doi:10.1016/S0021-9258(18)63139-4. PMID 5442268. https://doi.org/10.1016%2FS0021-9258%2818%2963139-4 ↩

  4. 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. PMID 8916922. /wiki/Doi_(identifier) ↩

  5. 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. PMID 9914247. /wiki/Doi_(identifier) ↩

  6. 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. PMID 9818189. /wiki/Doi_(identifier) ↩

  7. 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. PMID 10387030. /wiki/Doi_(identifier) ↩

  8. Thoden JB, Huang X, Raushel FM, Holden HM (October 2002). "Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia". The Journal of Biological Chemistry. 277 (42): 39722–7. doi:10.1074/jbc.M206915200. PMID 12130656. https://doi.org/10.1074%2Fjbc.M206915200 ↩

  9. Inkling. "Unsupported Browser". Inkling. Retrieved 25 April 2018. https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and ↩

  10. Engelking LR. Pyrimidine biosynthesis. Textbook of Veterinary Physiological Chemistry. 2015;:83–7. https://doi.org/10.1016/B978-0-12-391909-0.50014-1 Retrieved 1 April 2023 https://doi.org/10.1016/B978-0-12-391909-0.50014-1 ↩

  11. Moreno-Morcillo M, Grande-García A, Ruiz-Ramos A, del Caño-Ochoa F, Boskovic J, Ramón-Maiques S (2017). "Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis". Structure. 25 (6): 912–923. doi:10.1016/j.str.2017.04.012. hdl:10261/166586. PMID 28591622. https://doi.org/10.1016%2Fj.str.2017.04.012 ↩