2',3'-cyclic-nucleotide 2'-phosphodiesterase
| 2′,3′-cyclic-nucleotide 2′-phosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.16 | ||||||||
| CAS no. | 9037-18-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 2′,3′-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) catalyzes the general reaction
- nucleoside 2′,3′-cyclic phosphate + H2O nucleoside 3′-phosphate
For example, the enzyme characterised from Escherichia coli, 2',3'-cyclic AMP is hydrolysed to 3'-adenylic acid:[1][2][3]
Similar activity has been found in preparations from Proteus mirabilis, bovine brain, and Vibrio alginolyticus.[4][5][6]
This enzyme is a hydrolase, specifically one acting on phosphoric diester bonds. The systematic name is nucleoside-2′,3′-cyclic-phosphate 3'-nucleotidohydrolase. Other names in use include ribonucleoside 2′,3′-cyclic phosphate diesterase, 2′,3′-cyclic AMP phosphodiesterase, 2′,3′-cyclic nucleotidase, cyclic 2′,3′-nucleotide 2′-phosphodiesterase, cyclic 2′,3′-nucleotide phosphodiesterase, 2′,3′-cyclic nucleoside monophosphate phosphodiesterase, 2′,3′-cyclic AMP 2′-phosphohydrolase, cyclic phosphodiesterase:3′-nucleotidase, 2′,3′-cyclic nucleotide phosphohydrolase, 2′:3′-cyclic phosphodiesterase, and 2′:3′-cyclic nucleotide phosphodiesterase:3'-nucleotidase.[7]
References
- ↑ 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 (10): 3412–9. doi:10.1016/S0021-9258(18)97738-0. 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 (10): 3420–4. doi:10.1016/S0021-9258(18)97739-2. PMID 14245397.
- ↑ Rao, Feng; Qi, Yaning; Murugan, Elavazhagan; Pasunooti, Swathi; Ji, Qiang (2010). "2′,3′-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: Implications for PDE screening". Biochemical and Biophysical Research Communications. 398 (3): 500–505. doi:10.1016/j.bbrc.2010.06.107. PMID 20599695.
- ↑ Center MS, Behal FJ (1968). "A cyclic phosphodiesterase with 3′-nucleotidase activity from Proteus mirabilis". J. Biol. Chem. 243 (1): 138–43. doi:10.1016/S0021-9258(18)99334-8. PMID 4295113.
- ↑ Olafson RW, Drummond GI, Lee JF (1969). "Studies on 2′,3'-cyclic nucleotide-3'-phosphohydrolase from brain". Can. J. Biochem. 47 (10): 961–6. doi:10.1139/o69-151. PMID 4310670.
- ↑ Unemoto T, Hayashi M (1969). "Chloride ion as a modifier of 2′,3′-cyclic phosphodiesterase purified from halophilic Vibrio alginolyticus". Biochim. Biophys. Acta. 171 (1): 89–102. doi:10.1016/0005-2744(69)90108-9. PMID 4303200.
- ↑ Enzyme 3.1.4.16 at KEGG Pathway Database.