Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća)
Izgled
Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća) | |||||||||
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Identifikatori | |||||||||
EC broj | 6.3.5.5 | ||||||||
CAS broj | 37233-48-0 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća) (EC 6.3.5.5, karbamoil-fosfatna sintetaza (glutaminska hidroliza), karbamil fosfatna sintetaza (glutamin), karbamoilfosfatna sintetaza II, glutamin-zavisna karbamil fosfatna sintetaza, karbamoil fosfatna sintetaza, CPS, ugljen-dioksid:L-glutamin amido-ligaza (formira ADP, karbamatna fosforilacija)) je enzim sa sistematskim imenom vodonik-karbonat:L-glutamin amido-ligaza (formira ADP, karbamatna fosforilacija).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2 ATP + L-glutamin + HCO3- + H2O 2 ADP + fosfat + L-glutamat + karbamoil fosfat (sveukupna reakcija)
- (1a) L-glutamin + H2O L-glutamat + NH3
- (1b) 2 ATP + HCO3- + NH3 2 ADP + fosfat + karbamoil fosfat
Produkt karbamoil fosfat je intermedijer u biosintezi arginina i pirimidinskih nukleotida.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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