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EC Tree
IUBMB Comments Also hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides. Similar reactions are carried out by EC 4.6.1.24 (ribonuclease T1) and EC 4.6.1.18 (pancreatic ribonuclease).
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rv0805, 2',3'-cyclic nucleotide phosphohydrolase, 2',3'-cyclic phosphodiesterase, 2',3'-cyclic nucleotide 2'-phosphodiesterase, 2',3'-camp phosphodiesterase, 2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase, yfce-c74h, 2',3'-cyclic-nucleotide 2'-phosphodiesterase, 2',3'-cyclic nucleotidase, 2':3'-cyclic phosphodiesterase,
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2',3'-cyclic AMP 2'-phosphohydrolase
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2',3'-cyclic AMP phosphodiesterase
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2',3'-cyclic nucleoside monophosphate phosphodiesterase
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2',3'-cyclic nucleotidase
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2',3'-cyclic nucleotide 2'-phosphodiesterase
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2',3'-cyclic nucleotide phosphohydrolase
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2',3'-cyclic phosphodiesterase
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2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase
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2':3'-cyclic phosphodiesterase
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cyclic 2',3'-nucleotide phosphodiesterase
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cyclic phosphodiesterase:3'-nucleotidase
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cyclic-2',3'-nucleotide 2'-phosphohydrolase
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phosphodiesterase, cyclic 2',3'-nucleotide 2'-
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ribonucleoside 2',3'-cyclic phosphate diesterase
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YfcE-C74H
the mutant enzyme is strictly specific for 2',3'-cNMP, the C74H mutation uniquely confers a gain of function in hydrolysis of 2',3'-cAMP
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hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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nucleoside-2',3'-cyclic-phosphate 3'-nucleotidohydrolase
Also hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides. Similar reactions are carried out by EC 4.6.1.24 (ribonuclease T1) and EC 4.6.1.18 (pancreatic ribonuclease).
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2',3'-cAMP + H2O
2'-AMP + 3'-AMP
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?
2',3'-cGMP + H2O
2'-GMP + 3'-GMP
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?
2'-AMP + H2O
adenosine + phosphate
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?
ADP + H2O
AMP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
CDP + H2O
CMP + phosphate
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?
CTP + H2O
CDP + phosphate
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?
diphosphate + H2O
2 phosphate
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?
NADP+ + H2O
NAD+ + phosphate
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?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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?
3'-AMP + H2O
adenosine + phosphate
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?
3'-CMP + H2O
cytidine + phosphate
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?
3'-GMP + H2O
guanosine + phosphate
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?
3'-UMP + H2O
uridine + phosphate
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?
bis-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
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?
cyclic 2',3'-AMP + H2O
3'-AMP
cyclic 2',3'-CMP + H2O
3'-CMP
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?
cyclic 2',3'-GMP + H2O
3'-GMP
cyclic 2',3'-UMP + H2O
3'-UMP
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?
cyclic 3',5'-AMP + H2O
5'-AMP
weak activity
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?
cyclic 3',5'-GMP + H2O
5'-GMP
weak activity
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?
cyclic 3',5'-UMP + H2O
5'-UMP
weak activity
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?
di-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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?
additional information
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cyclic 2',3'-AMP + H2O
3'-AMP
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cyclic 2',3'-AMP + H2O
3'-AMP
YfcE-C74H cleaves exclusively the P-O2' bond of 2',3'-cAMP
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cyclic 2',3'-GMP + H2O
3'-GMP
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?
cyclic 2',3'-GMP + H2O
3'-GMP
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?
di-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
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?
di-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
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at 50% of the activity with cyclic 2',3'-UMP
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?
additional information
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3'-nucleotidase and 5'-nucleotidase activity resides in the same protein
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?
additional information
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YfcE-C74H has no detectable ability to hydrolyze phosphomonoester substrates 5'-AMP, 3'-AMP, or 2'-AMP
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?
additional information
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YfcE-C74H has no detectable ability to hydrolyze phosphomonoester substrates 5'-AMP, 3'-AMP, or 2'-AMP
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?
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Mg2+
activataes with 2'-AMP, KD: 0.24 +/- 0.1 mM
Mg2+
activates with 2',3'-cAMP, KD: 0.49 +/- 0.1 mM
Mg2+
activates with ATP, KD ~ 0.1 mM
Ni2+
activates with diphosphate, KD: 1.06 +/- 0.1 uM
Ni2+
activates with p-nitrophenyl phosphate, KD: 6.0 +/- 0.7 uM
Co2+
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activates
Co2+
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0.1-1 mM, 3-5fold activation
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Zn2+
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0.1
diphosphate
+/- 0.004
6.2
p-nitrophenyl phosphate
+/- 0.46
0.28
bis(p-nitrophenyl)phosphate
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9.3
bis-p-nitrophenyl phosphate
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
35
cyclic 2',3'-AMP
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
6
p-nitrophenyl phosphate
in Tris-HCl buffer (pH 8.5) in the presence of 5 mM MnCl2
additional information
additional information
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2.51
diphosphate
+/- 0.05
10.3
p-nitrophenyl phosphate
+/- 0.28
72
bis-p-nitrophenyl phosphate
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
2.95
cyclic 2',3'-AMP
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
3
p-nitrophenyl phosphate
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
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0.29
tRNA
with ATP
1.68
tRNA
with 2',3'-cAMP
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2.5
phosphate
Escherichia coli
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12.4
+/- 0.34, p-nitrophenyl phosphate
2.36
+/- 0.10, 2',3'-cGMP
3.01
+/- 0.06, diphosphate
additional information
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5 - 6.5
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hydrolysis of di-p-nitrophenyl phosphate
6.4
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6.4
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3'-nucleotidase activity and cyclic phosphodiesterase activity against cyclic 2',3'-UMP
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SwissProt
brenda
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brenda
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H98A
the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate
H98D
the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate
H98N
the mutation suppresses the 2',3'-cAMP phosphodiesterase specific activity to one-fifth the level of wild type Rv0805
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70
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5 min, loss of activity
55
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inactivation
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4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
2-4°C, pH 7.4-7.6, Tris buffer, 20-30% loss of activity after 2 months
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Ni-NTA agarose column chromatography
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expressed in Escherichia coli strain BL21(DE3)
genetic mapping of the cpdB locus
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Drummond, G.I.; Yamamoto, M.
Nucleoside cyclic phosphate diesterases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
355-371
1971
Bacillus subtilis, Enterobacter sp., Escherichia coli, Escherichia coli B / ATCC 11303, Proteus mirabilis, Proteus vulgaris, Salmonella enterica subsp. enterica serovar Heidelberg, Serratia marcescens, Shigella sonnei, Vibrio alginolyticus
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brenda
Beacham, I.R.; Garrett, S.
Isolation of Escherichia coli mutants (cpdB) deficient in periplasmic 2:3-cyclic phosphodiesterase and genetic mapping of the cpdB locus
J. Gen. Microbiol.
119
31-34
1980
Escherichia coli
brenda
Anraku, Y.
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
1964
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Anraku, Y.
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
1964
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Yakunin, A.F.; Proudfoot, M.; Kuznetsova, E.; Savchenko, A.; Brown, G.; Arrowsmith, C.H.; Edwards, A.M.
The HD domain of the E. coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities
J. Biol. Chem.
279
36819-36827
2004
Escherichia coli (P06961), Escherichia coli
brenda
Keppetipola, N.; Shuman, S.
A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2,3-cyclic nucleotide phosphodiesterase activity
J. Biol. Chem.
283
30942-30949
2008
Escherichia coli (P67095), Escherichia coli, Mycobacterium tuberculosis
brenda