Carbamoyl phosphate synthase II

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Carbamoyl-phosphate synthetase (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
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PMC articles
PubMed articles
NCBI proteins
carbamoyl-phosphate synthetase 1, aspartate transcarbamylase, and dihydroorotase
Identifiers
SymbolCAD
NCBI gene 790
HGNC 1424
OMIM 114010
RefSeq NM_004341
UniProt P27708
Other data
Locus Chr. 2 p21
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Structures Swiss-model
Domains InterPro

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]

Contents

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

  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): 2803–2809. doi:10.1021/bi00888a034. PMID   5326356.
  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): 1871–1877. doi: 10.1016/S0021-9258(18)96716-5 . PMID   5329589.
  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): 2199–2204. doi: 10.1016/S0021-9258(18)63139-4 . PMID   5442268.
  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): 14352–14361. doi:10.1021/bi961183y. PMID   8916922.
  5. ↑ Holden HM, Thoden JB, Raushel FM (December 1998). "Carbamoyl phosphate synthetase: a tunnel runs through it". Current Opinion in Structural Biology. 8 (6): 679–685. doi:10.1016/s0959-440x(98)80086-9. PMID   9914247.
  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): 624–632. doi:10.1016/s1367-5931(98)80094-x. PMID   9818189.
  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): 7891–7899. doi:10.1021/bi990871p. PMID   10387030.
  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): 39722–39727. doi: 10.1074/jbc.M206915200 . PMID   12130656.
  9. ↑ Inkling. "Unsupported Browser". Inkling. Retrieved 25 April 2018.
  10. ↑ Engelking LR (2015). "Pyrimidine biosynthesis.". Textbook of Veterinary Physiological Chemistry. pp. 83–87. doi:10.1016/B978-0-12-391909-0.50014-1 . Retrieved 1 April 2023.
  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.


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