The Enzyme Database

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EC 3.1.4.37     
Accepted name: 2′,3′-cyclic-nucleotide 3′-phosphodiesterase
Reaction: nucleoside 2′,3′-cyclic phosphate + H2O = nucleoside 2′-phosphate
Other name(s): cyclic-CMP phosphodiesterase; 2′,3′-cyclic AMP phosphodiesterase; cyclic 2′,3′-nucleotide 3′-phosphodiesterase; cyclic 2′,3′-nucleotide phosphodiesterase; 2′,3′-cyclic nucleoside monophosphate phosphodiesterase; 2′,3′-cyclic nucleotide 3′-phosphohydrolase; CNPase; 2′,3′-cyclic nucleotide phosphohydrolase; 2′:3′-cyclic nucleotide 3′-phosphodiesterase; 2′:3′-CNMP-3′-ase
Systematic name: nucleoside-2′,3′-cyclic-phosphate 2′-nucleotidohydrolase
Comments: The brain enzyme acts on 2′,3′-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2′,3′-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3′,5′-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60098-35-3
References:
1.  Drummond, G.I., Iyer, N.T. and Keith, J. Hydrolysis of ribonucleoside 2′,3′-cyclic phosphates by a diesterase from brain. J. Biol. Chem. 237 (1962) 3535–3539.
2.  Helfman, D.M. and Kuo, J.F. A homogeneous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2′:3′- and 3′:5′-nucleotides. J. Biol. Chem. 257 (1982) 1044–1047. [PMID: 6274851]
3.  Helfman, D.M., Shoji, M. and Kuo, J.F. Purification to homogeneity and general properties of a novel phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP. J. Biol. Chem. 256 (1981) 6327–6334. [PMID: 6263914]
4.  Kurihara, T., Nishizawa, Y., Takahashi, Y. and Odani, S. Chemical, immunological and catalytic properties of 2′:3′-cyclic nucleotide 3′-phosphodiesterase purified from brain white matter. Biochem. J. 195 (1981) 153–157. [PMID: 6272743]
5.  Nishizawa, Y., Kurihara, T. and Takahashi, Y. Spectrophotometric assay, solubilization and purification of brain 2′:3′-cyclic nucleotide 3′-phosphodiesterase. Biochem. J. 191 (1980) 71–82. [PMID: 6258586]
[EC 3.1.4.37 created 1976]
 
 


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