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Information on EC 3.1.4.16 - 2',3'-cyclic-nucleotide 2'-phosphodiesterase and Organism(s) Escherichia coli and UniProt Accession P06961

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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).
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This record set is specific for:
Escherichia coli
UNIPROT: P06961
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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, yfce-c74h, 2',3'-cyclic-nucleotide 2'-phosphodiesterase, 2',3'-cyclic nucleotidase, 2':3'-cyclic phosphodiesterase, cyclic 2',3'-nucleotide phosphodiesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9037-18-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-cAMP + H2O
2'-AMP + 3'-AMP
show the reaction diagram
-
-
-
?
2',3'-cGMP + H2O
2'-GMP + 3'-GMP
show the reaction diagram
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
show the reaction diagram
-
-
-
?
cyclic 2',3'-AMP + H2O
3'-AMP
show the reaction diagram
cyclic 2',3'-CMP + H2O
3'-CMP
show the reaction diagram
-
-
-
-
?
cyclic 2',3'-GMP + H2O
3'-GMP
show the reaction diagram
cyclic 2',3'-UMP + H2O
3'-UMP
show the reaction diagram
-
-
-
-
?
cyclic 3',5'-AMP + H2O
5'-AMP
show the reaction diagram
weak activity
-
-
?
cyclic 3',5'-GMP + H2O
5'-GMP
show the reaction diagram
weak activity
-
-
?
cyclic 3',5'-UMP + H2O
5'-UMP
show the reaction diagram
weak activity
-
-
?
di-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
dependent on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.49
2',3'-cAMP
+/- 0.04
1.6
2',3'-cGMP
+/- 0.22
0.76
2'-AMP
+/- 0.13
0.19
ADP
+/- 0.02
0.18
ATP
+/- 0.01
0.53
CDP
+/- 0.09
0.13
CTP
+/- 0.01
0.1
diphosphate
+/- 0.004
0.15
NADP
+/- 0.02
6.2
p-nitrophenyl phosphate
+/- 0.46
0.05
3'-AMP
-
-
0.053
3'-UMP
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-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.63
2',3'-cAMP
+/- 0.48
1.97
2',3'-cGMP
+/- 0.08
3.09
2'-AMP
+/- 0.14
1.24
ADP
+/- 0.07
3.78
ATP
+/- 0.12
4.83
CDP
+/- 0.39
3.36
CTP
+/- 0.17
2.51
diphosphate
+/- 0.05
14.9
NADP
+/- 0.5
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 1.68
tRNA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
phosphate
Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.49
+/- 0.08, ADP
12.4
+/- 0.34, p-nitrophenyl phosphate
17.9
+/- 0.6, NADP
2.36
+/- 0.10, 2',3'-cGMP
3.01
+/- 0.06, diphosphate
3.21
+/- 0.1, 2',3'-cAMP
3.71
+/- 0.17, 2'-CMP
4.03
+/- 0.20, CTP
4.53
+/- 0.14, ATP
5.8
+/- 0.47, CDP
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
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hydrolysis of di-p-nitrophenyl phosphate
7.5 - 8
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7.6 - 8.3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
predominantly
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
5 min, loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)
genetic mapping of the cpdB locus
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team