Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća)
| Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 6.3.5.5 | ||||||||
| CAS broj | 37233-48-0 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | 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.
Reference
[уреди | уреди извор]- ^ Anderson, P.M. & 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. & 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.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- Carbamoyl-phosphate+synthase+(glutamine-hydrolysing) на US National Library of Medicine Medical Subject Headings (MeSH)
