Carbamoyl phosphate synthase II
| Carbamoyl-phosphate synthase (glutamine-hydrolysing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.5.5 | ||||||||
| CAS no. | 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 2, 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 II EC 6.3.5.5, carbamoyl-phosphate synthetase (glutamine-hydrolysing), carbamyl phosphate synthetase (glutamine), carbamoylphosphate synthetase II, glutamine-dependent carbamyl phosphate synthetase, carbamoyl phosphate synthetase, CPS, carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)) is an enzyme that catalyzes the reactions that produce carbamoyl phosphate in the cytosol (as opposed to type I, which functions in the mitochondria). It 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 catalyzes the following reaction:
- 2 ATP + L-glutamine + HCO3- + H2O 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction)
- (1a) L-glutamine + H2O L-glutamate + NH3
- (1b) 2 ATP + HCO3- + NH3 2 ADP + phosphate + carbamoyl phosphate
It is activated by ATP and PRPP and it is inhibited by UMP (Uridine monophosphate, the end product of the pyrimidine synthesis pathway).
Neither CPSI nor CPSII require biotin as a coenzyme, as seen with most carboxylation reactions.
It is one of the three enzyme functions coded by the CAD gene. It is classified under EC 6.3.5.5.
References
- ^ Anderson, P.M. and Meister, A. (1965). "Evidence for an activated form of carbon dioxide in the reaction catalysed by Escherichia coli carbamyl phosphate synthetase". Biochemistry. 4: 2803–2809. PMID 5326356.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kalman, S.M., Duffield, P.H. and Brzozowski, T. (1966). "Purification and properties of a bacterial carbamyl phosphate synthetase". J. Biol. Chem. 241: 1871–1877. PMID 5329589.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yip, M.C.M. and Knox, W.E. (1970). "Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues". J. Biol. Chem. 245: 2199–2204. PMID 5442268.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Stapleton, M.A., Javid-Majd, F., Harmon, M.F., Hanks, B.A., Grahmann, J.L., Mullins, L.S. and Raushel, F.M. (1996). "Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase". Biochemistry. 35: 14352–14361. PMID 8916922.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Holden, H.M., Thoden, J.B. and Raushel, F.M. (1998). "Carbamoyl phosphate synthetase: a tunnel runs through it". Curr. Opin. Struct. Biol. 8: 679–685. PMID 9914247.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Raushel, F.M., Thoden, J.B., Reinhart, G.D. and Holden, H.M. (1998). "Carbamoyl phosphate synthetase: a crooked path from substrates to products". Curr. Opin. Chem. Biol. 2: 624–632. PMID 9818189.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Raushel, F.M., Thoden, J.B. and Holden, H.M. (1999). "The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia". Biochemistry. 38: 7891–7899. PMID 10387030.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Thoden, J.B., Huang, X., Raushel, F.M. and Holden, H.M. (2002). "Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia". J. Biol. Chem. 277: 39722–39727. PMID 12130656.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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