Carbamoyl phosphate synthase II: Difference between revisions

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'''Carbamoyl phosphate synthetase II''' ({{EC number|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)''.<ref>{{cite journal | title = Evidence for an activated form of carbon dioxide in the reaction catalysed by ''Escherichia coli'' carbamyl phosphate synthetase |author1 = Anderson, P.M. |author2 =Meister, A. |journal = Biochemistry |year = 1965 |volume = 4 |pages = 2803–2809 |pmid = 5326356 |issue=12 |doi=10.1021/bi00888a034}}</ref><ref>{{cite journal | title = Purification and properties of a bacterial carbamyl phosphate synthetase |author1 = Kalman, S.M. |author2 =Duffield, P.H. |author3 =Brzozowski, T. |journal = J. Biol. Chem. |year = 1966 |volume = 241 |pages = 1871–1877 |pmid = 5329589 |issue=8}}</ref><ref>{{cite journal | title = Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues |author1 = Yip, M.C.M. |author2 =Knox, W.E. |journal = J. Biol. Chem. |year = 1970 |volume = 245 |pages = 2199–2204 |pmid = 5442268 |issue=9}}</ref><ref>{{cite journal | title = Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase |author1 = Stapleton, M.A. |author2 =Javid-Majd, F. |author3 =Harmon, M.F. |author4 =Hanks, B.A. |author5 =Grahmann, J.L. |author6 =Mullins, L.S. |author7 =Raushel, F.M. | journal = Biochemistry |year = 1996 |volume = 35 |pages = 14352–14361 |pmid = 8916922 |doi=10.1021/bi961183y}}</ref><ref>{{cite journal | title = Carbamoyl phosphate synthetase: a tunnel runs through it |author1 = Holden, H.M. |author2 =Thoden, J.B. |author3 =Raushel, F.M. |journal = Curr. Opin. Struct. Biol. |year = 1998 |volume = 8 |pages = 679–685 |pmid = 9914247 |issue=6 |doi=10.1016/s0959-440x(98)80086-9}}</ref><ref>{{cite journal | title = Carbamoyl phosphate synthetase: a crooked path from substrates to products |author1 = Raushel, F.M. |author2 =Thoden, J.B. |author3 =Reinhart, G.D. |author4 =Holden, H.M. |journal = Curr. Opin. Chem. Biol. |year = 1998 |volume = 2 |pages = 624–632 |pmid = 9818189 |issue=5 |doi=10.1016/s1367-5931(98)80094-x}}</ref><ref>{{cite journal | title = The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia |author1 = Raushel, F.M. |author2 =Thoden, J.B. |author3 =Holden, H.M. |journal = Biochemistry |year = 1999 |volume = 38 |pages = 7891–7899 |pmid = 10387030 |doi=10.1021/bi990871p}}</ref><ref>{{cite journal | title = Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia |author1 = Thoden, J.B. |author2 =Huang, X. |author3 =Raushel, F.M. |author4 =Holden, H.M. |journal = J. Biol. Chem. |year = 2002 |volume = 277 |pages = 39722–39727 |pmid = 12130656 |doi=10.1074/jbc.M206915200 |issue=42}}</ref>
'''Carbamoyl phosphate synthetase II''' ({{EC number|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)''.<ref>{{cite journal | vauthors = Anderson PM, Meister A | title = Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase | journal = Biochemistry | volume = 4 | issue = 12 | pages = 2803–9 | date = December 1965 | pmid = 5326356 | doi = 10.1021/bi00888a034 }}</ref><ref>{{cite journal | vauthors = Kalman SM, Duffield PH, Brzozowski T | title = Purification and properties of a bacterial carbamyl phosphate synthetase | journal = The Journal of Biological Chemistry | volume = 241 | issue = 8 | pages = 1871–7 | date = April 1966 | pmid = 5329589 }}</ref><ref>{{cite journal | vauthors = Yip MC, Knox WE | title = Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues | journal = The Journal of Biological Chemistry | volume = 245 | issue = 9 | pages = 2199–204 | date = May 1970 | pmid = 5442268 }}</ref><ref>{{cite journal | vauthors = Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL, Mullins LS, Raushel FM | title = Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase | journal = Biochemistry | volume = 35 | issue = 45 | pages = 14352–61 | date = November 1996 | pmid = 8916922 | doi = 10.1021/bi961183y }}</ref><ref>{{cite journal | vauthors = Holden HM, Thoden JB, Raushel FM | title = Carbamoyl phosphate synthetase: a tunnel runs through it | journal = Current Opinion in Structural Biology | volume = 8 | issue = 6 | pages = 679–85 | date = December 1998 | pmid = 9914247 | doi = 10.1016/s0959-440x(98)80086-9 }}</ref><ref>{{cite journal | vauthors = Raushel FM, Thoden JB, Reinhart GD, Holden HM | title = Carbamoyl phosphate synthetase: a crooked path from substrates to products | journal = Current Opinion in Chemical Biology | volume = 2 | issue = 5 | pages = 624–32 | date = October 1998 | pmid = 9818189 | doi = 10.1016/s1367-5931(98)80094-x }}</ref><ref>{{cite journal | vauthors = Raushel FM, Thoden JB, Holden HM | title = The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia | journal = Biochemistry | volume = 38 | issue = 25 | pages = 7891–9 | date = June 1999 | pmid = 10387030 | doi = 10.1021/bi990871p }}</ref><ref>{{cite journal | vauthors = Thoden JB, Huang X, Raushel FM, Holden HM | title = Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia | journal = The Journal of Biological Chemistry | volume = 277 | issue = 42 | pages = 39722–7 | date = October 2002 | pmid = 12130656 | doi = 10.1074/jbc.M206915200 }}</ref>


In [[pyrimidine]] biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:
In [[pyrimidine]] biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:
Line 35: Line 35:
: (1b) 2 ATP + HCO<sub>3</sub><sup>−</sup> + NH<sub>3</sub> <math>\rightleftharpoons</math> 2 ADP + phosphate + carbamoyl phosphate
: (1b) 2 ATP + HCO<sub>3</sub><sup>−</sup> + NH<sub>3</sub> <math>\rightleftharpoons</math> 2 ADP + phosphate + carbamoyl phosphate


It is activated by [[Adenosine triphosphate|ATP]] and [[PRPP]]<ref>https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and</ref> and it is inhibited by UMP ([[Uridine monophosphate]], the end product of the pyrimidine synthesis pathway).   
It is activated by [[Adenosine triphosphate|ATP]] and [[PRPP]]<ref>{{cite web|url=https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and|title=Unsupported Browser|first=|last=Inkling|date=|website=Inkling|accessdate=25 April 2018}}</ref> 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.   
Neither CPSI nor CPSII require [[biotin]] as a coenzyme, as seen with most carboxylation reactions.   
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* CPS
* CPS
* carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)
* carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)
 
{{clear}}
== References ==
== References ==
{{reflist}}
{{reflist|32em}}


==External links==
== External links ==
* {{MeshName|Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing)}}
* {{MeshName|Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing)}}


Latest revision as of 14:08, 25 April 2018

Carbamoyl-phosphate synthetase (glutamine-hydrolysing)
Identifiers
EC number6.3.5.5
CAS number37233-48-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
carbamoyl-phosphate synthetase 1, aspartate transcarbamylase, and dihydroorotase
Identifiers
SymbolCAD
Entrez790
HUGO1424
OMIM114010
RefSeqNM_004341
UniProtP27708
Other data
LocusChr. 2 p21

Carbamoyl phosphate synthetase II (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 + HCO3− + H2O <math>\rightleftharpoons</math> 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction)
(1a) L-glutamine + H2O <math>\rightleftharpoons</math> L-glutamate + NH3
(1b) 2 ATP + HCO3− + NH3 <math>\rightleftharpoons</math> 2 ADP + phosphate + carbamoyl phosphate

It is activated by ATP and PRPP[9] 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.

Nomenclature

Carbamoyl-phosphate synthetase (glutamine-hydrolysing) is also known as:

  • hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)
  • carbamyl phosphate synthetase (glutamine)
  • glutamine-dependent carbamyl phosphate synthetase
  • carbamoyl phosphate synthetase
  • CPS
  • carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)

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.
  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. 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): 2199–204. 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): 14352–61. 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): 679–85. 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): 624–32. 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): 7891–9. 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): 39722–7. doi:10.1074/jbc.M206915200. PMID 12130656.
  9. ↑ Inkling. "Unsupported Browser". Inkling. Retrieved 25 April 2018.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Carbamoyl_phosphate_synthase_II&oldid=1531491"