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Information on EC 3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase and Organism(s) Escherichia coli and UniProt Accession P06961

for references in articles please use BRENDA:EC3.1.4.37
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IUBMB 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.
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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: Eukaryota, Bacteria, Archaea
Synonyms
cnpase, 2',3'-cyclic nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide 3'-phosphohydrolase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphohydrolase, 2':3'-cyclic nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide phosphodiesterase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase type i, 2':3'-cnmp-3'-ase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2',3'-cyclic AMP phosphodiesterase
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2',3'-cyclic nucleoside monophosphate phosphodiesterase
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2',3'-cyclic nucleotide 3'-phosphohydrolase
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2',3'-cyclic nucleotide phosphohydrolase
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2':3'-cyclic nucleotide 3'-phosphodiesterase
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CNP
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-
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CNPase
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cyclic 2',3'-nucleotide 3'-phosphodiesterase
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cyclic 2',3'-nucleotide phosphodiesterase
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cyclic-CMP phosphodiesterase
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nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase
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phosphodiesterase, cyclic 2',3'-nucleotide 3'-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
nucleoside-2',3'-cyclic-phosphate 2'-nucleotidohydrolase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
60098-35-3
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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
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
cyclic 2',3'-CMP + H2O
2'-CMP
show the reaction diagram
low activity
-
?
cyclic 2',3'-GMP + H2O
2'-GMP
show the reaction diagram
high activity
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
natural substrate, the 2',3'-cyclic phosphodiesterase activity of the C-terminal HD domain of tRNA nucleotidyltransferase, EC 2.7.7.25, is involved in the repair of the 3’-CCA end of tRNA
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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
0.49
cyclic 2',3'-AMP
pH 7, 37°C
1.6
cyclic 2',3'-GMP
pH 7, 37°C
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
0.031 - 7.63
cyclic 2',3'-AMP
1.97 - 2.94
cyclic 2',3'-GMP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 1.68
tRNA
0.00000168
tRNA
hydrolysis of cyclic 2',3'-AMP
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
predominantly
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D21A
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D23A
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D256A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
D306A
HD domain mutant with 2',3'-cyclic phosphodiesterase activity
H225A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
H305A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase 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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Escherichia coli (P06961)
Manually annotated by BRENDA team