2',3'-cyclic-nucleotide 2'-phosphodiesterase

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is nucleoside-2',3'-cyclic-phosphate 3'-nucleotidohydrolase. Other names in common 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. This enzyme participates in purine metabolism and pyrimidine metabolism.

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: 3412–9. 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: 3420–4. PMID 14245397.
Center MS, Behal FJ (1968). "A cyclic phosphodiesterase with 3'-nucleotidase activity from Proteus mirabilis". J. Biol. Chem. 243 (1): 138–43. 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.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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