Information on EC 3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.4.37
-
RECOMMENDED NAME
GeneOntology No.
2',3'-cyclic-nucleotide 3'-phosphodiesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. amyloliquefacus
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
zebrafish
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Rattus norvegicus
in olfactory ensheathing cells
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
bullfrog
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
polynucleotide kinase-phosphatase
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
role of 2',3'-cyclic nucleotide 3'-phosphodiesterase in the renal 2',3'-cAMP-adenosine pathway, overview
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-etheno-2-azaadenosine-2',3'-cyclic monophosphate + H2O
etheno-2-azaadenosine-2'-monophosphate
show the reaction diagram
-
-
-
-
?
1,N6-ethenoadenosine-2',3'-cyclic monophosphate + H2O
ethenoadenosine-2'-monophosphate
show the reaction diagram
-
-
-
-
?
2', 3'-cyclic ribonucleotide
ribonucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
2',3'-cAMP + H2O
2'-AMP + 3'-AMP
show the reaction diagram
-
-
-
-
2',3'-cAMP + H2O
3'-AMP + ?
show the reaction diagram
-
the exclusive formation of 3'-AMP is due to the P-O2' bond having lower activation energy and is not the result of steric exclusion at enzyme active site, kinetic evidence that hydrolysis of 2',3'-cAMP into 3'-AMP is nonspecific. Modeling of 2',3'-cyclic nucleotide into the active site of a EAL domain PDE, overview
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
2',3'-cGMP + H2O
2'-GMP + 3'-GMP
show the reaction diagram
-
-
-
-
2',3'-cNADP+ + H2O
2'-NADP+
show the reaction diagram
2',3'-cNADP+ + H2O
?
show the reaction diagram
-
-
-
?
2',3'-cNADP+ + H2O
NADP+
show the reaction diagram
-
-
-
?
2',3'-cUMP + H2O
2'-UMP
show the reaction diagram
2',3'-cyclic AMP + H2O
2'-AMP
show the reaction diagram
2',3'-cyclic NADP+ + H2O
NADP+
show the reaction diagram
2',3'-cyclic-2-aza-e-AMP + H2O
2'-2-aza-e-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cyclic-e-AMP + H2O
2'-e-AMP
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
3'-AMP + H2O
?
show the reaction diagram
-
-
-
-
?
adenosine 2,3-cyclic phosphorothioate + H2O
?
show the reaction diagram
the Sp epimer of 2',3'-cAMPS is a functional substrate for the enzyme, while the Rp epimer is not
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
bis(p-nitrophenyl)phosphate + H2O
?
show the reaction diagram
-
non-specific substrate
-
-
?
bis-p nitrophenyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
CTP + H2O
CDP + phosphate
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
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
NADP+ + H2O
NAD+ + phosphate
show the reaction diagram
-
-
-
-
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
nucleoside 2',3'-cyclic phosphates + H2O
?
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2',3'-cyclic AMP + H2O
2'-AMP
show the reaction diagram
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
P06961
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
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
nucleoside 2',3'-cyclic phosphates + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activation of activity against bis-p-nitrophenyl phosphate
Ni2+
activates with p-nitrophenyl phosphate, KD: 6.0 +/- 0.7 uM; activates with PPi, KD: 1.06 +/- 0.1 uM; hydrolysis of bis-p-nitrophenyl phosphate is strongly dependent on Ni2+
sulfate
-
two sulfate molecules are located in the vicinity of the catalytic site, the active-site sulfate mimics the substrate phosphate group and interacts with all 4 conserved residues of the two HxTx motifs and the two central water molecules in the catalytic site through H-bonds, being also in contact with the backbone carbonyl of Pro320 and bulk solvent. The second sulfate stabilizes the long alpha6-beta5 loop
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-AMP
3',5'-cAMP
-
-
5'-AMP
5,5'-dithiobis-(2-nitrobenzoic acid)
-
97% inhibition of the catalytic fragment of CNP1 in a time- and dose-dependent manner, kinetics, fully reversed by excess dithiothreitol or 2-mercaptoethanol, inhibition is attributable to steric effects of modification of Cys-236 and Cys-314 by the inhibitor
adenosine
-
-
arsenate
-
-
arsenite
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-
Atractyloside
-
noncompetitive
basic fibroblast growth factor
-
-
-
Ca2+
-
74% inhibition at 0.5 mM
Caffeine
Diethylpyrocarbonate
-
pH 6.5, 22C, time-dependent inhibition, kinetics, completely reversed by 0.5 M hydroxylamine
diisopropyl fluoroacetate
-
-
Elastase
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little inactivation
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Fe3+
-
66% inhibition at 0.5 mM
Guanidinium chloride
-
-
heparin
iodoacetamide
-
-
KCN
-
62% inhibition of the catalytic fragment of CNP1
lead
-
90 days exposure of young adult rats to lead in drinking water, decrease both in enzyme protein content and activity
methyl mercury
-
-
methyl methanethiosulfonate
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42% inhibition of the catalytic fragment of CNP1
NaCH3COO
-
-
p-chloromercuribenzoate
-
98% inhibition at 0.2 mM
physostygmine
-
-
Polynucleotides
Sulfhydryl reagent
-
-
-
theophylline
thimerosal
tRNA
10 nM, strong competitive inhibition of 2',3'-cyclic phosphodiesterase activity, inhibition is abolished by addition of Mg2+, Mn2+ or Ca2+, but not of Ni2+
Trypsin
tubercidin
-
-
Zn(CH3COO)2
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
cytosine arabinoside
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-
Digitonin
-
-
EDTA
-
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Hexadecyltrimethylammonium bromide
-
-
histone F3
lipopolysaccharide
-
enzyme expression is significantly up-regulated in microglial activation induced in vitro by lipopolysaccharide
Lubrol WX
-
-
-
myelin basic protein
Na-deoxycholate
protein activator
-
-
-
Triton X-100
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
1,N6-Etheno-2-azaadenosine-2',3'-cyclic monophosphate
-
-
8.3
1,N6-Ethenoadenosine-2',3'-cyclic monophosphate
-
rat brain
0.25 - 13.1
2',3'-cAMP
0.8 - 25.2
2',3'-cCMP
0.57 - 9.2
2',3'-cGMP
0.098 - 0.55
2',3'-cNADP
8.3 - 25.3
2',3'-cUMP
0.553 - 1.305
2',3'-Cyclic AMP
0.76
2'-AMP
+/- 0.13
0.046
3'-AMP
-
-
0.19
ADP
+/- 0.02
0.18
ATP
+/- 0.01
0.16
bis-p-nitrophenyl phosphate
-
-
0.53
CDP
+/- 0.09
0.13
CTP
+/- 0.01
0.49 - 100
cyclic 2',3'-AMP
1.6
cyclic 2',3'-GMP
pH 7, 37C
0.1
diphosphate
+/- 0.004
0.15
NADP
+/- 0.02
6.2
p-nitrophenyl phosphate
+/- 0.46
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.63 - 118
2',3'-cAMP
1.97
2',3'-cGMP
Escherichia coli
P06961
+/- 0.08
1.15 - 1690
2',3'-cNADP
14 - 940
2',3'-Cyclic AMP
3.09
2'-AMP
Escherichia coli
P06961
+/- 0.14
1.24
ADP
Escherichia coli
P06961
+/- 0.07
3.78
ATP
Escherichia coli
P06961
+/- 0.12
4.83
CDP
Escherichia coli
P06961
+/- 0.39
3.36
CTP
Escherichia coli
P06961
+/- 0.17
0.031 - 34.3
cyclic 2',3'-AMP
1.97 - 2.94
cyclic 2',3'-GMP
2.51
diphosphate
Escherichia coli
P06961
+/- 0.05
14.9
NADP
Escherichia coli
P06961
+/- 0.5
10.3
p-nitrophenyl phosphate
Escherichia coli
P06961
+/- 0.28
additional information
additional information
Bos taurus
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
220
2',3'-cAMP
Mus musculus
-
full-length protein
942
10 - 1700
2',3'-Cyclic AMP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
2'-AMP
-
-
0.00000168 - 1.68
tRNA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.066
-
rabbit, adrenal gland
0.133
-
2',3'-cAMP, hole mitochondria
0.24
-
mitochondrial inner membrane
0.28
-
mitochondrial outer membrane
1.49
+/- 0.08, ADP
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
6.28
-
2',3 '-cCMP, fish retina
11.2
-
pH 6.2, 37, treatment with lead
12.4
+/- 0.34, p-nitrophenyl phosphate
13.4
-
pH 6.2, 37C
17.9
+/- 0.6, NADP
35
-
2',3'-cAMP, frog brain
130.6
-
ZRICH-WT-enzyme
280
-
2',3'-cGMP
600
-
2',3'-cUMP
800 - 2000
2090
-
2',3'-cAMP
2140
-
2',3'-cCMP
2300
-
-
2680
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
activity against bis-p-nitrophenyl phosphate
5.4 - 6.2
-
without detergent
6 - 7
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-
6.1 - 6.7
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-
6.6
-
-
8 - 8.3
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6.5
-
-
4 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.3
-
isoelectric focusing
9
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
9.2
-
theoretical value
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
glioma cells
Manually annotated by BRENDA team
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presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
Manually annotated by BRENDA team
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cerebellar, both isoforms CNP1 and CNP2
Manually annotated by BRENDA team
-
ubiquitinated CNP
Manually annotated by BRENDA team
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DRG explant cultures
Manually annotated by BRENDA team
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ATCC CRL 8305, thyroid cells, CNP is firmly associated with FRTL-5 cells
Manually annotated by BRENDA team
-
encysted
Manually annotated by BRENDA team
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olfactory bulb ensheathing glia in explant cultures
Manually annotated by BRENDA team
quantitative isozymes expression analysis in hepatoma cell lines
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
peripheral nerve sheath tumors, immunohistochemic and histochemic analysis of 63 tumors from 44 cattle: 35 schwannomas, 9 neurofibromas, 14 hybrid (neurofibroma-schwannoma) tumors, and 5 malignant peripheral nerve sheath tumors
Manually annotated by BRENDA team
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peripheral nerve sheath tumors, immunohistochemic and histochemic analysis of 63 tumors from 44 cattle: 35 schwannomas, 9 neurofibromas, 14 hybrid (neurofibroma-schwannoma) tumors, and 5 malignant peripheral nerve sheath tumors
Manually annotated by BRENDA team
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3 weeks old
Manually annotated by BRENDA team
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
Manually annotated by BRENDA team
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myelin sheaths of the cerebral white matter
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
tubulin from brain, microtubule-associated protein, membrane anchor for tubulin, membrane-bound
Manually annotated by BRENDA team
-
rod outer segment
Manually annotated by BRENDA team
additional information