- Nomenclature
- References
- External links
| Name = Carbamoyl-phosphate synthetase (glutamine-hydrolysing)
| EC_number = 6.3.5.5
| CAS_number = 37233-48-0
| IUBMB_EC_number = 6/3/5/5
| GO_code =
| image =
| width =
| caption =
}}{{protein
|Name=carbamoyl-phosphate synthetase 1, aspartate transcarbamylase, and dihydroorotase
|caption=
|image=
|width=
|HGNCid=1424
|Symbol=CAD
|AltSymbols=
|EntrezGene=790
|OMIM=114010
|RefSeq=NM_004341
|UniProt=P27708
|PDB=
|ECnumber=
|Chromosome=2
|Arm=p
|Band=21
|LocusSupplementaryData=
}}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).[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− + H2O2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction)
(1a) L-glutamine + H2O
(1b) 2 ATP + HCO3− + NH3
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 number|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. ^{{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 }}
2. ^{{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 }}
3. ^{{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 }}
4. ^{{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 }}
5. ^{{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 }}
6. ^{{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 }}
7. ^{{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 }}
8. ^{{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 }}
9. ^{{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}}
2. ^{{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 }}
3. ^{{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 }}
4. ^{{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 }}
5. ^{{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 }}
6. ^{{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 }}
7. ^{{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 }}
8. ^{{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 }}
9. ^{{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}}
External links
- {{MeshName|Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing)}}
1 : EC 6.3.5
- Carbonyldiamine
- Carbonyl dibromide
- Carbonyl dichloride
- Carbonyl difluoride
- Carbonyl ligand
- Carbonyl metallurgy
- Carbonyl Metallurgy
- Carbonyl nickel
- Carbonyl oxidation with hypervalent iodine reagents
- Carbonyl Process
- Carbonyl process
- Carbonyl reduction
- Carbon-zinc
- Carbon zinc battery
- Carbon zinc cell battery
- Carboprost tromethamine
- Carboquone
- Carborexia
- Carbos
- Carbosilfocon a
- Carbo, Sonora
- Carbosphaerella
- Carbost
- Carbost, Isle of Skye
- Carbost, Loch Harport