Fosforibozilaminoimidazolsukcinokarboksamidna sintaza
Izgled
Fosforibozilaminoimidazolsukcinokarboksamidna sintaza | |||||||||
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Fosforibozilaminoimidazolsukcinokarboksamidna sintetaza oktamer, Human | |||||||||
Identifikatori | |||||||||
EC broj | 6.3.2.6 | ||||||||
CAS broj | 9023-67-0 | ||||||||
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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Fosforibozilaminoimidazolsukcinokarboksamidna sintaza (EC 6.3.2.6, fosforibozilaminoimidazol-sukcinokarboksamidna sintetaza, PurC, SAICAR sintetaza, 4-(N-sukcinokarboksamid)-5-aminoimidazolna sintetaza, 4-((N-sukcinilamino)karbonil)-5-aminoimidazol ribonukleotidna sintetaza, SAICARs, fosforibozilaminoimidazolsukcinokarboksamidna sintetaza, 5-aminoimidazol-4-N-sukcinokarboksamid ribonukleotid sintetaza) je enzim sa sistematskim imenom 5-amino-1-(5-fosfo-D-ribozil)imidazol-4-karboksilat:L-aspartat ligaza (formira ADP).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + 5-amino-1-(5-fosfo-D-ribozil)imidazol-4-karboksilat + L-aspartat ADP + fosfat + (S)-2-[5-amino-1-(5-fosfo-D-ribozil)imidazole-4-karboksamido]sukcinat
Ovaj enzim učestvuje u purinskoj biosintezi.
- ↑ Lukens, L.N. and Buchanan, J.M. (1959). „Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5′-phosphate from 5-amino-1-ribosylimidazole 5′-phosphate and carbon dioxide”. J. Biol. Chem. 234: 1799-1805. PMID 13672967.
- ↑ Parker, J. (1984). „Identification of the purC gene product of Escherichia coli”. J. Bacteriol. 157: 712-717. PMID 6365889.
- ↑ Ebbole, D.J. and Zalkin, H. (1987). „Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis”. J. Biol. Chem. 262: 8274-8287. PMID 3036807.
- ↑ Chen, Z.D., Dixon, J.E. and Zalkin, H. (1990). „Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by functional complementation of Escherichia coli pur mutants”. Proc. Natl. Acad. Sci. USA 87: 3097-3101. PMID 1691501.
- ↑ O'Donnell, A.F., Tiong, S., Nash, D. and Clark, D.V. (2000). „The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme for two steps in the de novo purine synthesis pathway”. Genetics 154: 1239-1253. PMID 10757766.
- ↑ Nelson, S.W., Binkowski, D.J., Honzatko, R.B. and Fromm, H.J. (2005). „Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase”. Biochemistry 44: 766-774. PMID 15641804.
- 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.