2',3'-Ciklični-nukleotid 2'-fosfodiestaraza
| 2',3'-Ciklični-nukleotid 2'-fosfodiestaraza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.4.16 | ||||||||
| CAS broj | 9037-18-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
2',3'-Ciklični-nukleotid 2'-fosfodiestaraza (EC 3.1.4.16, ribonukleozid 2',3'-ciklična fosfat diesteraza, 2',3 '-ciklična AMP fosfodiesteraza, 2',3'-ciklična nukleotidaza, ciklična 2',3'-nukleotid 2'-fosfodiesteraza, ciklična 2',3'-nukleotid fosfodiesteraza, 2',3'-ciklična nukleozid monofosfat fosfodiesteraza, 2',3'-ciklična AMP 2'-fosfohidrolaza, ciklična fosfodiesteraza:3'-nukleotidaza, 2',3'-ciklična nukleotid fosfohidrolaza, 2':3'-ciklična fosfodiesteraza, 2':3'-ciklična nukleotid fosfodiesteraza:3'-nukleotidaza) je enzim sa sistematskim imenom nukleozid-2',3'-ciklična-fosfat 3'-nukleotidohidrolaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- nukleozid 2',3'-ciklični fosfat + H2O nukleozid 3'-fosfat
Ovaj enzim takođe hidrolizuje 3'-nukleozid monofosfate i bis-4-nitrofenil fosfate.
- ↑ Anraku, Y. (1964). „A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B. I. Purification and some properties of the enzyme”. J. Biol. Chem. 239: 3412-3419. PMID 14245396.
- ↑ Anraku, Y. (1964). „A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B. II. Further studies on substrate specificity and mode of action of the enzyme”. J. Biol. Chem. 239: 3420-3424. PMID 14245397.
- ↑ Center, M.S. and Behal, F.J. (1968). „A cyclic phosphodiesterase with 3′-nucleotidase activity from Proteus mirabilis”. J. Biol. Chem. 243: 138-143. PMID 4295113.
- ↑ Olafson, R.W., Drummond, G.I. and Lee, J.F. (1969). „Studies on 2′,3′-cyclic nucleotide-3′-phosphohydrolase from brain”. Can. J. Biochem. 47: 961-966. PMID 4310670.
- ↑ Unemoto, T. and Hayashi, M. (1969). „Chloride ion as a modifier of 2′,3′-cyclic phosphodiesterase purified from halophilic Vibrio alginolyticus”. Biochim. Biophys. Acta 171: 89-102. PMID 4303200.
- 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.