Biology:Carbamoyl phosphate synthase II
| Carbamoyl-phosphate synthetase (glutamine-hydrolysing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.5.5 | ||||||||
| CAS number | 37233-48-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| carbamoyl-phosphate synthetase 1, aspartate transcarbamylase, and dihydroorotase | |
|---|---|
| Identifiers | |
| Symbol | CAD |
| NCBI gene | 790 |
| HGNC | 1424 |
| OMIM | 114010 |
| RefSeq | NM_004341 |
| UniProt | P27708 |
| Other data | |
| Locus | Chr. 2 p21 |
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).[1][2][3][4][5][6][7][8]
In pyrimidine biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:
- 2 ATP + L-glutamine + HCO−
3 + H2O ⇌ 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction) - (1a) L-glutamine + H2O ⇌ L-glutamate + NH3
- (1b) 2 ATP + HCO−
3 + NH3 ⇌ 2 ADP + phosphate + carbamoyl phosphate
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 EC 6.3.5.5.
See also
References
- ↑ "Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase". Biochemistry 4 (12): 2803–2809. December 1965. doi:10.1021/bi00888a034. PMID 5326356.
- ↑ "Purification and properties of a bacterial carbamyl phosphate synthetase". The Journal of Biological Chemistry 241 (8): 1871–1877. April 1966. doi:10.1016/S0021-9258(18)96716-5. PMID 5329589.
- ↑ "Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues". The Journal of Biological Chemistry 245 (9): 2199–2204. May 1970. doi:10.1016/S0021-9258(18)63139-4. PMID 5442268.
- ↑ "Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase". Biochemistry 35 (45): 14352–14361. November 1996. doi:10.1021/bi961183y. PMID 8916922.
- ↑ "Carbamoyl phosphate synthetase: a tunnel runs through it". Current Opinion in Structural Biology 8 (6): 679–685. December 1998. doi:10.1016/s0959-440x(98)80086-9. PMID 9914247.
- ↑ "Carbamoyl phosphate synthetase: a crooked path from substrates to products". Current Opinion in Chemical Biology 2 (5): 624–632. October 1998. doi:10.1016/s1367-5931(98)80094-x. PMID 9818189.
- ↑ "The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia". Biochemistry 38 (25): 7891–7899. June 1999. doi:10.1021/bi990871p. PMID 10387030.
- ↑ "Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia". The Journal of Biological Chemistry 277 (42): 39722–39727. October 2002. doi:10.1074/jbc.M206915200. PMID 12130656.
- ↑ Inkling. "Unsupported Browser". https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and.
- ↑ "Pyrimidine biosynthesis.". Textbook of Veterinary Physiological Chemistry. 2015. pp. 83–87. doi:10.1016/B978-0-12-391909-0.50014-1. https://doi.org/10.1016/B978-0-12-391909-0.50014-1. Retrieved 1 April 2023.
- ↑ "Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis". Structure 25 (6): 912–923. 2017. doi:10.1016/j.str.2017.04.012. PMID 28591622.
External links
- Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing) at the US National Library of Medicine Medical Subject Headings (MeSH)
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