Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća)
| Karbamoil-fosfatna sintaza (glutamin-hidrolizujuća) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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
- ↑ 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.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Carbamoyl-phosphate+synthase+(glutamine-hydrolysing)
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
