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Information on EC 3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase
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3.1.4.37 2',3'-cyclic-nucleotide 3'-phosphodiesteraseIUBMB 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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Word Map
- 3.1.4.37
- myelin
- oligodendrocyte
- glial
- mbp
- matter
- astrocyte
- nerve
- demyelination
- cord
-
fibrillary
- sclerosis
-
myelin-associated
- sheath
-
proteolipid
- cerebral
- oligodendroglial
-
corpus
-
schwann
- callosum
- sulfatide
- microglia
- nestin
- galactocerebroside
-
sciatic
-
3\'-cyclic
-
myelin-specific
-
myelin-related
-
hypomyelination
- 5'-nucleotidase
-
myelinogenesis
- neurofilament
- galactolipids
- medicine
- diagnostics
-
luxol
-
ensheathing
- cuprizone
-
quaking
- cerebroside
-
paranodal
-
jimpy
-
cuprizone-induced
-
shiverer
-
myelin-like
-
myelin-forming
-
oligodendrocyte-specific
- analysis
-
oligodendrogenesis
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2',3'-cyclic AMP phosphodiesterase
-
-
-
-
2',3'-cyclic nucleoside monophosphate phosphodiesterase
-
-
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
2',3'-cyclic nucleotide 3'-phosphohydrolase
-
-
-
-
2',3'-cyclic nucleotide phosphodiesterase
2',3'-cyclic nucleotide phosphohydrolase
-
-
-
-
2':3'-CNMP-3'-ase
2':3'-cyclic nucleotide 3'-phosphodiesterase
-
-
-
-
CNP
CNP1
CNPase
cyclic 2',3'-nucleotide 3'-phosphodiesterase
-
-
-
-
cyclic 2',3'-nucleotide phosphodiesterase
-
-
-
-
cyclic-CMP phosphodiesterase
-
-
-
-
nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase
-
-
-
-
phosphodiesterase, cyclic 2',3'-nucleotide 3'-
-
-
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
CNP
-
-
-
-
CNPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
-
-
-
-
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
catalytic mechanism
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
general acid/general base catalysis by H310, H231 and a water molecule, mechanism
-
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
during catalytic mechanism, a 2',3'-cyclic nucleotide is converted into a 2'-nucleotide through a nucleophilic attack carried out by an activated water molecule, dinucleotide binding mode, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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.
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CAS REGISTRY NUMBER
COMMENTARY
60098-35-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,N6-etheno-2-azaadenosine-2',3'-cyclic monophosphate + H2O
etheno-2-azaadenosine-2'-monophosphate
-
-
-
-
?
1,N6-ethenoadenosine-2',3'-cyclic monophosphate + H2O
ethenoadenosine-2'-monophosphate
-
-
-
-
?
2',3'-cAMP + H2O
3'-AMP + ?
-
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
-
-
?
adenosine 2,3-cyclic phosphorothioate + H2O
?
the Sp epimer of 2',3'-cAMPS is a functional substrate for the enzyme, while the Rp epimer is not
-
-
?
2',3'-cAMP + H2O
2'-AMP
-
the protein consists of two domains: an uncharacterized N-terminal domain with little homology to other proteins, and a C-terminal phosphodiesterase domain. C-terminal tail (22 residues) has no significant effect on the catalytic activity, neither do the first 24 N-terminal residues of the full-length protein. Both the N- and C-terminal domain of recombinant CNPase are folded entities: N-terminal domain has more beta-sheet structure and less alpha-helices than the C-terminal domain
-
-
?
2',3'-cyclic AMP + H2O
2'-AMP
substrate and product enzyme binding structures, overview
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
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
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
dinucleotide binding mode, overview
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
activity resides in the C-terminus
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
His-230 and His-309 of CNP1 play critical roles in enzyme catalysis, no essential role of cysteines, the catalytic domain forms a compact globular structure
-
ir
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
plays a role in cytoskeletal rearrangement, cell morphology and cell process outgrowth, increased expression of CNP is a marker for oligodendrocyte development
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
additional information
?
-
-
not: nucleoside 3',5'-cyclic phosphate
-
?
additional information
?
-
not: nucleoside 3',5'-cyclic phosphate
-
?
additional information
?
-
-
endogenous Nogo-A interacts with the endogenous CNP in vitro and in vivo
-
-
?
additional information
?
-
-
the cAMP-mediated pathway is part of the molecular mechanisms regulating the expression of CNP1 in oligodendrocytes, roles of AP-2, AP-4 and nuclear factor-1 in the regulation of CNP1 expression
-
?
additional information
?
-
-
enzyme is involved in mediating process formation in oligodendrocytes
-
-
?
additional information
?
-
-
CNP acts as microtubule-associated protein in promoting microtubule assembly at low mole ratios, links tubulin to membranes and may regulate cytoplasmic microtubule distribution, membrane anchor for tubulin
-
?
additional information
?
-
-
CNP is one of the earliest myelin-related proteins to be expressed in differentiated oligodendrocytes and Schwann cells, role in migration and/or expansion of membranes during myelination
-
?
additional information
?
-
-
CNP performs an integral role in myelinogenesis, both isoforms likely play complementary roles in the onset of process outgrowth and ultimately myelination of axons
-
?
additional information
?
-
-
early oligodendroglial marker, CNPase links myelin related proteins to the cytoskeleton also interacting with membrane lipids during extension and wrapping of the oligodendroglial process around the axon, in mature myelinated fiber the CNPase is absent from compact myelin sheath, being located only in the inner and outer loops and in paranodal loops
-
?
additional information
?
-
-
myelin-specific protein, synthesized by oligodendrocytes, more abundant in the myelin of the CNS than in that of the peripheral nervous system, CNP is regulated by several protein kinases and may have a role in morphological changes of the cells by modulating the cytoskeleton
-
?
additional information
?
-
-
non-compact myelin protein, may have a unique role in signaling pathways mediated by lipid-protein domains
-
?
additional information
?
-
-
related to axonal ensheathment by myelinating cells
-
?
additional information
?
-
-
the cAMP-mediated pathway is part of the molecular mechanisms regulating the expression of CNP1 in oligodendrocytes, roles of AP-2, AP-4, nuclear factor-1 and protein kinase A in the regulation of CNP1 expression
-
?
additional information
?
-
-
endogenous enzyme expression is augmented by juxtanodin transfection, an oligodendroglial protein that promotes cellular arborization. Juxtanodin also augments transport of enzyme to the process arbors of cultured primary oligodendrocyte precursors
-
-
?
additional information
?
-
-
enzyme can perform the essential 3'-end-healing steps of tRNA splicing in yeast and complement growth of strains bearing lethal or temperature-sensitive mutations in the tRNA ligase 3'-end-healing domain
-
-
?
additional information
?
-
-
enzyme binds purine nucleotide triphosphates with an affinity higher than that displayed for diphosphates, while the affinity for both purine monophosphates and pyrimidine nucleotides is negligible. Analysis of binding constants for GTP, GDP, GMP, ATP, ADP, CTP, CDP, UTP, UDP
-
-
?
additional information
?
-
-
CNP is an RNA-binding protein, CNP associates with poly(A)+ mRNAs in vivo and suppresses translation in vitro in a dose-dependent manner, isoform CNP1 may regulate expression of mRNAs in oligodendrocytes of the central nervous system
-
-
?
additional information
?
-
-
substrate specificities and activities of RocR, DGC2, YybT, YtqI, 3DMA, and PaAcpH with 2',3'-cAMP, overview
-
-
?
additional information
?
-
-
not: 2',3'-cyclic esters in cyclic phosphate-terminated oligoribonucleotides or in nucleoside 5'-phosphate, 2',3'-cyclic phosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclic 2',3'-AMP + H2O
2'-AMP
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
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
plays a role in cytoskeletal rearrangement, cell morphology and cell process outgrowth, increased expression of CNP is a marker for oligodendrocyte development
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
-
-
-
-
?
additional information
?
-
-
the cAMP-mediated pathway is part of the molecular mechanisms regulating the expression of CNP1 in oligodendrocytes, roles of AP-2, AP-4 and nuclear factor-1 in the regulation of CNP1 expression
-
?
additional information
?
-
-
enzyme is involved in mediating process formation in oligodendrocytes
-
-
?
additional information
?
-
-
CNP acts as microtubule-associated protein in promoting microtubule assembly at low mole ratios, links tubulin to membranes and may regulate cytoplasmic microtubule distribution, membrane anchor for tubulin
-
?
additional information
?
-
-
CNP is one of the earliest myelin-related proteins to be expressed in differentiated oligodendrocytes and Schwann cells, role in migration and/or expansion of membranes during myelination
-
?
additional information
?
-
-
CNP performs an integral role in myelinogenesis, both isoforms likely play complementary roles in the onset of process outgrowth and ultimately myelination of axons
-
?
additional information
?
-
-
early oligodendroglial marker, CNPase links myelin related proteins to the cytoskeleton also interacting with membrane lipids during extension and wrapping of the oligodendroglial process around the axon, in mature myelinated fiber the CNPase is absent from compact myelin sheath, being located only in the inner and outer loops and in paranodal loops
-
?
additional information
?
-
-
myelin-specific protein, synthesized by oligodendrocytes, more abundant in the myelin of the CNS than in that of the peripheral nervous system, CNP is regulated by several protein kinases and may have a role in morphological changes of the cells by modulating the cytoskeleton
-
?
additional information
?
-
-
non-compact myelin protein, may have a unique role in signaling pathways mediated by lipid-protein domains
-
?
additional information
?
-
-
related to axonal ensheathment by myelinating cells
-
?
additional information
?
-
-
the cAMP-mediated pathway is part of the molecular mechanisms regulating the expression of CNP1 in oligodendrocytes, roles of AP-2, AP-4, nuclear factor-1 and protein kinase A in the regulation of CNP1 expression
-
?
additional information
?
-
-
endogenous enzyme expression is augmented by juxtanodin transfection, an oligodendroglial protein that promotes cellular arborization. Juxtanodin also augments transport of enzyme to the process arbors of cultured primary oligodendrocyte precursors
-
-
?
additional information
?
-
-
enzyme can perform the essential 3'-end-healing steps of tRNA splicing in yeast and complement growth of strains bearing lethal or temperature-sensitive mutations in the tRNA ligase 3'-end-healing domain
-
-
?
additional information
?
-
-
CNP is an RNA-binding protein, CNP associates with poly(A)+ mRNAs in vivo and suppresses translation in vitro in a dose-dependent manner, isoform CNP1 may regulate expression of mRNAs in oligodendrocytes of the central nervous system
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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
Ca2+
-
Ca2+-stimulated and permeability transition pore-associated enzyme phosphorylation
Ni2+
hydrolysis of bis-p-nitrophenyl phosphate is strongly dependent on Ni2+
additional information
-
metal-independent 2',3'-cyclic phosphodiesterase activity
additional information
metal-independent 2',3'-cyclic phosphodiesterase activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-dipropyl-8-(4-sulfophenyl)xanthine
-
41% inhibition at 1 mM, 75% inhibition at 10 mM
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
diethylpyrocarbonate
-
pH 6.5, 22°C, time-dependent inhibition, kinetics, completely reversed by 0.5 M hydroxylamine
lead
-
90 days exposure of young adult rats to lead in drinking water, decrease both in enzyme protein content and activity
methyl methanethiosulfonate
-
42% inhibition of the catalytic fragment of CNP1
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+
additional information
-
effect of ethanol on the activity and expression of CNP isoenzymes, ethanol does not alter the developmentally regulated increased expression of CNP isoenzymes or enzyme activity
-
additional information
-
hypothyroidism impairs transiently the CNPase gene expression, rats receiving methimazol during gestation or postnatally show a delay in CNPase expression followed by a decrease in the number of CNPase immunoreactive fibers
-
additional information
-
actinomycin D or cycloheximide completely inhibits the dibutyryl-cAMP-induced accumulation of CNP1 mRNA
-
additional information
-
no effect on enzyme activity by calmodulin binding
-
additional information
-
not inhibited by 1 mM 3-isobutyl-1-methylxanthine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
-
enzyme expression is significantly up-regulated in microglial activation induced in vitro by lipopolysaccharide
additional information
-
up-regulation of CNP1 expression by cAMP or its analogues, e.g. dibutyryl-cAMP, in C6 cells transfected with mouse CNP1 gene
-
additional information
-
up-regulation of CNP1 expression compared with CMP2 expression by cAMP or its analogues, e.g. dibutyryl-cAMP, in C6 cells
-
additional information
-
no effect on enzyme activity by calmodulin binding
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.295
2',3'-cNADP
-
pH 6, 25°C, catalytic fragment of CNP1 corresponding to the C-terminal 250 amino acids
0.483
2',3'-cNADP+
mutant enzyme P225G, pH and temperature not specified in the publication
0.553
2',3'-cNADP+
wild type enzyme, pH and temperature not specified in the publication
0.722
2',3'-cNADP+
mutant enzyme P296G, pH and temperature not specified in the publication
1.045
2',3'-cNADP+
mutant enzyme V321A, pH and temperature not specified in the publication
1.055
2',3'-cNADP+
mutant enzyme H230Q, pH and temperature not specified in the publication
1.192
2',3'-cNADP+
mutant enzyme H309S, pH and temperature not specified in the publication
1.305
2',3'-cNADP+
mutant enzyme H230S, pH and temperature not specified in the publication
1.385
2',3'-cNADP+
mutant enzyme Y168S, pH and temperature not specified in the publication
1.879
2',3'-cNADP+
mutant enzyme Y168A, pH and temperature not specified in the publication
2.192
2',3'-cNADP+
mutant enzyme R307Q, pH and temperature not specified in the publication
3.788
2',3'-cNADP+
mutant enzyme F235L, pH and temperature not specified in the publication
6.253
2',3'-cNADP+
mutant enzyme F235A, pH and temperature not specified in the publication
39.648
2',3'-cNADP+
mutant enzyme T232A, pH and temperature not specified in the publication
0.553
2',3'-Cyclic AMP
wild-type enzyme, pH and temperature not specified in the publication
1.045
2',3'-Cyclic AMP
mutant V321A, pH and temperature not specified in the publication
1.055
2',3'-Cyclic AMP
mutant H230Q, pH and temperature not specified in the publication
1.192
2',3'-Cyclic AMP
mutant H309S, pH and temperature not specified in the publication
1.305
2',3'-Cyclic AMP
mutant H230S, pH and temperature not specified in the publication
additional information
additional information
-
in the prescence of serum albumin or hexadecyltrimethylammonium bromide
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1690
2',3'-cNADP
-
pH 6, 25°C, catalytic fragment of CNP1 corresponding to the C-terminal 250 amino acids
14
2',3'-cNADP+
mutant enzyme H230S, pH and temperature not specified in the publication
21
2',3'-cNADP+
mutant enzyme H309S, pH and temperature not specified in the publication
24
2',3'-cNADP+
mutant enzyme H230Q, pH and temperature not specified in the publication
183
2',3'-cNADP+
mutant enzyme F235A, pH and temperature not specified in the publication
221
2',3'-cNADP+
mutant enzyme F235L, pH and temperature not specified in the publication
231
2',3'-cNADP+
mutant enzyme T232A, pH and temperature not specified in the publication
237
2',3'-cNADP+
mutant enzyme Y168A, pH and temperature not specified in the publication
732
2',3'-cNADP+
mutant enzyme V321A, pH and temperature not specified in the publication
887
2',3'-cNADP+
mutant enzyme Y168S, pH and temperature not specified in the publication
940
2',3'-cNADP+
wild type enzyme, pH and temperature not specified in the publication
1182
2',3'-cNADP+
mutant enzyme R307Q, pH and temperature not specified in the publication
1332
2',3'-cNADP+
mutant enzyme P296G, pH and temperature not specified in the publication
1420
2',3'-cNADP+
mutant enzyme P225G, pH and temperature not specified in the publication
14
2',3'-Cyclic AMP
mutant H230S, pH and temperature not specified in the publication
21
2',3'-Cyclic AMP
mutant H309S, pH and temperature not specified in the publication
24
2',3'-Cyclic AMP
mutant H230Q, pH and temperature not specified in the publication
732
2',3'-Cyclic AMP
mutant V321A, pH and temperature not specified in the publication
940
2',3'-Cyclic AMP
wild-type enzyme, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
2',3'-cNADP+
Kcat_Km less than 10 1/sec*mM, mutant enzyme T232A, pH and temperature not specified in the publication
10
2',3'-cNADP+
mutant enzyme H230S, pH and temperature not specified in the publication
20
2',3'-cNADP+
mutant enzyme H230Q, pH and temperature not specified in the publication
20
2',3'-cNADP+
mutant enzyme H309S, pH and temperature not specified in the publication
30
2',3'-cNADP+
mutant enzyme F235A, pH and temperature not specified in the publication
60
2',3'-cNADP+
mutant enzyme F235L, pH and temperature not specified in the publication
130
2',3'-cNADP+
mutant enzyme Y168A, pH and temperature not specified in the publication
540
2',3'-cNADP+
mutant enzyme R307Q, pH and temperature not specified in the publication
640
2',3'-cNADP+
mutant enzyme Y168S, pH and temperature not specified in the publication
700
2',3'-cNADP+
mutant enzyme V321A, pH and temperature not specified in the publication
1700
2',3'-cNADP+
wild type enzyme, pH and temperature not specified in the publication
1730
2',3'-cNADP+
mutant enzyme P296G, pH and temperature not specified in the publication
2940
2',3'-cNADP+
mutant enzyme P225G, pH and temperature not specified in the publication
10
2',3'-Cyclic AMP
mutant H230S, pH and temperature not specified in the publication
20
2',3'-Cyclic AMP
mutant H230Q, pH and temperature not specified in the publication
20
2',3'-Cyclic AMP
mutant H309S, pH and temperature not specified in the publication
700
2',3'-Cyclic AMP
mutant V321A, pH and temperature not specified in the publication
1700
2',3'-Cyclic AMP
wild-type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
800 - 2000
additional information
additional information
-
mitochondrial inner and outer membrane, effect of chronic ethanol ingestion
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
2',3'-cyclic phosphodiesterase activity of the C-terminal HD domain of the multifunctional enzyme tRNA nucleotidyltransferase, EC 2.7.7.25
-
-
brenda
-
-
-
brenda
two isozymes, difference between the variants is the presence of a 20-amino-acid N-terminal mitochondrial targeting sequence in the 48-kDa isoform II, which is removed after mitochondrial import to produce a truncated 46-kDa variant that corresponds to the cytosolic isoform I of 400 amino-acids, gene CNP1
-
-
brenda
-
135396, 135399, 135401, 135404, 135407, 135408, 135413, 135418, 135419, 135420, 135422, 653684, 668237, 670668, 678336, 679178, 681551, 682134, 682844, 693783, 714030, 729185, 729954, 730239, 730475
-
-
brenda
2 isoforms: CNP1 and CNP2 differing by a 20-amino acid extension at the N-terminus
-
-
brenda
Sprague-Dawley rats, 1-2 days old, 2 isoforms: CNP1 and CNP2 differing by a 20-amino acid extension exclusive to CNP2
-
-
brenda
Sprague-Dawley rats, adult, 2 isoforms: CNP1 and CNP2, produced by ribosome initiation at different AUG codons
-
-
brenda
Wistar and Lister strains, age ranging from postnatal day 3 to 60
-
-
brenda
Wistar rats, from post-natal days 5 to 90, hypothyroid and controls
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
brenda
-
ATCC CRL 8305, thyroid cells, CNP is firmly associated with FRTL-5 cells
brenda
quantitative isozymes expression analysis in hepatoma cell lines
brenda
-
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
brenda
-
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
brenda
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
brenda
additional information
-
-
brenda
-
two enzyme isoforms in chicken, just one isoform in bullfrog
brenda
-
-
135380, 135381, 135399, 135401, 135404, 135407, 135418, 135419, 135422, 729185, 729954, 730238, 730475, 751698
brenda
-
CNPase expression pattern of brain tissues in hypothyroid and control rats from post-natal days 5 to 90, hypothyroidism impairs transiently the CNPase gene expression, effect on oligodendrocyte differentiation and myelination
brenda
-
subventricular zone rostral extension, CNPase expression pattern during development from postnatal day 3 to 60
brenda
-
there is little CNP2 in the forebrain postsynaptic density fraction, CNP1 is the major isoform in the neural and non-neural rat tissues, with the exception of myelinating cells in the adult brain, in which both isoforms are highly expressed, CNP2 is barely detectable in embryonic brain
brenda
-
amoeboid microglial cells in the postnatal rat brain
-
brenda
-
cerebellar postsynaptic density fraction, both isoforms CNP1 and CNP2 are expressed in cerian populations of cerebellar cells, in oligodendrocytes, Purkinje cells and unidentified PSD95-positive cells, not in granule cells
brenda
-
with age, CNP accumulates throughout brain white matter accompanied by proteolytic fragments of CNP. Equal increase in both isoforms CNP1 and CNP2
brenda
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
brenda
-
oligodendrocyte-enriched cultures of neonatal rat brain glial cells, CNP2
brenda
the enzyme is expressed in liver tissues with hepatitis B virus infection
brenda
-
with age, CNP accumulates in myelin accompanied by proteolytic fragments of CNP. Equal increase in both isoforms CNP1 and CNP2
brenda
-
the enzyme is most abundant protein in non-compact myelin and the third-most abundant protein overall in CNS myellin
brenda
a highly abundant membrane-associated enzyme in the myelin sheath of the vertebrate nervous system
brenda
-
the enzyme is one of the most abundant proteins in CNS myelin
brenda
-
the enzyme is one of the most abundant proteins in CNS myelin
brenda
-
the enzyme is a quantitatively major enzyme in myelin, where it localizes to the non-compact regions and is bound to the membrane surface
brenda
-
the enzyme is one of the most abundant proteins in CNS myelin
brenda
-
developing, detailed CNPase expression pattern during development from postnatal day 3 to 60, expression follows a general caudorostral gradient, with the exception of the glomerular layer
brenda
-
olfactory bulb ensheathing glia in explant cultures
brenda
-
olfactory ensheathing cells, the nonmyelinating glial cells of the olfactory nerves and bulb, in situ immunohistochemic analysis, overview
brenda
-
bipotential proliferating and differentiating CG-4 cells
brenda
-
the two isoforms CNP1 and CNP2 are differentially regulated during the process of maturation, CNP expression pattern
brenda
-
myelinating, colocalization of CNPase and CaM during Schwann cell myelination in culture
brenda
additional information
-
bovine peripheral nerve sheath tumors commonly have both schwannomatous and neurofibromatous areas
brenda
additional information
-
variety of cultured cells and cell lines
brenda
additional information
-
spatiotemporal distribution of CNPase, an early oligodendrocyte/Schwann cell marker, overview
brenda
additional information
-
variety of cultured cells and cell lines
brenda
additional information
-
variety of cultured cells and cell lines
brenda
additional information
-
CNP2 is barely detectable in testis and thymus
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
tubulin from brain, microtubule-associated protein, membrane anchor for tubulin, membrane-bound
brenda
additional information
-
abundantly in the cytoplasmic compartments of CNS myelin
brenda
-
along the cytoplasmic boundaries of the normal oligodendroglia. Mild to moderate anti-CNPase staining extends to the swollen cytoplasm of the oligodendroglia in aniline-treated rats from day 2 to day 4
brenda
-
exclusively associated with the cytosolic side of the membrane
brenda
-
single and double-unit membrane, from non-compact regions of myelin
brenda
-
membrane-anchored enzyme present on the cytosolic side of non-compact myelin
brenda
-
integral membrane protein, inner and outer mitochondrial membrane
brenda
-
membrane-bound, microtubule-associated protein, membrane anchor for tubulin
brenda
-
a 13 residue C-terminal fragment is responsible for enzyme membrane anchoring. Lipidation of the 13 residue fragment is essential for the peptide to be folded and correctly positioned on the membrane surface
brenda
the N-terminus ofisozyme CNP2 serves as a mitochondrial targeting signal and translocates it to the mitochondrion
brenda
-
enzyme contains a mitochondrial targeting signal at the N-terminus. Import to mitochondria leads to cleavage of signal sequence yielding a mature, truncated form of CNP2 similar in size as CNP1. CNP2 is localized specifically to mitochondria in non-myelinating cells, e.g. in adult liver or embryonic brain. Phosphorylation of the signal sequence by protein kinase C inhibits translocation to mitochondria.
brenda
-
distribution of isozymes in mitochondrial fractions, i.e. myelin fraction, synaptic and nonsynaptic mitochondria, obtained after separation of brain mitochondria
brenda
-
the enzyme is associated with complexes I-V in mitochondria
brenda
-
distribution of isozymes in mitochondrial fractions, i.e. myelin fraction, synaptic and nonsynaptic mitochondria, obtained after separation of brain mitochondria
-
brenda
additional information
-
ubiquitinated CNP in the Triton X-100 insoluble lipid raft associated fractions of myelin
-
brenda
additional information
-
the enzyme binds to calmodulin in a Ca2+-dependent manner via its binding site in the N-terminal domain, colocalization of CNPase and CaM during Schwann cell myelination in culture, molecular modeling
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms
evolution
-
the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms
evolution
-
the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms
evolution
-
the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms
evolution
the enzyme is a unique member of the 2H phosphoesterase family. 2H phosphoesterases differ in their respective reaction mechanisms despite the conserved catalytic residues. The HxS/Tx motifs of the catalytic phosphodiesterase domain are conserved throughout species, domains structure comparison, overview. Conservation of ligand-binding residues
evolution
the enzyme is a unique member of the 2H phosphoesterase family. Large differences in the active-site vicinity are observed when comparing more distant members of the 2H family
malfunction
-
a C-terminally truncated variant of CNPase, as well as a mutant unable to membrane-associate, are affected in oligodendrocyte process outgrowth, formation and branching
malfunction
-
changes in enzyme expression levels are linked to Alzheimer's disease, Down's syndrome, and catatonia-depression syndrome. A single-nucleotide polymorphism that does not alter the amino-acid sequence of the enzyme, but rather decreases its expression levels, has been suggested to play a role in schizophrenia
malfunction
-
inducible nitric oxide synthase, IL-1beta, TNF-alpha, reactive oxygen species and nitric oxide are significantly upregulated in activated BV-2 cells with CNPase enzyme knockdown. siRNA knockdown of the enzyme increases microglia migration, on the other hand, microglial cells appear to be arrested at G1 phase
malfunction
knockdown of the enzyme expression moderately improves hepatitis B viral production in the HepG2.2.15 cells treated with IFN-alpha
malfunction
-
truncations after amino acid 164 in recombinant rat enzyme result in a loss of phosphodiesterase activity
malfunction
-
enzyme deletion attenuates ischemia-reperfusion-induced acute kidney injury, in part by accelerating autophagy with targeted removal of damaged mitochondria
metabolism
-
role of 2',3'-cyclic nucleotide 3'-phosphodiesterase in the renal 2',3'-cAMP-adenosine pathway, overview
metabolism
-
the enzyme is involved in the regulation of the kinases Akt and GSK3beta
physiological function
-
an age-related impairment in proteasomal proteolysis and subsequent accumulation of ubiquitinated CNP activates alternative proteolytic mechanisms leading to CNP fragmentation
physiological function
-
an age-related impairment in proteasomal proteolysis and subsequent accumulation of ubiquitinated CNP activates alternative proteolytic mechanisms leading to CNP fragmentation. In the aged monkey, CNP is ubiquitinated and this ubiquitination can be found (at least in part) in detergent insoluble membrane microdomains
physiological function
-
incomplete degradation of CNP due to failure of the proteasomal system and aberrant degradation by calpain-1 leads to agerelated CNP accumulation and proteolysis. These phenomena result in age-related dysfunction of CNP in the lipid raft, which may lead to myelin and axonal pathology
physiological function
-
the CNP gene may not be involved in the etiology and pathology of schizophrenia in the Chinese Han population. No significant association between the two polymorphisms rs2070106 and rs8078650 and schizophrenia
physiological function
-
CNP is a cell type-specific marker of oligodendrocytes, has a physiological relevance to axon, myelin and oligodendrocytes, and acts as a conformational stabilizer for the intrinsically unstructured large segment of Amino-Nogo
physiological function
-
Ca2+-stimulated and permeability transition pore-associated enzyme phosphorylation might be an important stage of permeability transition pore regulation in mitochondria, revealing an additional function of CNPase outside of myelin structure
physiological function
-
in early stages of myelination, the enzyme is essential in oligodendrocyte process formation and branching, as well as for oligodendrocyte process outgrowth via its membrane association, as well as its ability to interact with the cytoskeleton. The role of CNPase after active myelination is related to axonal maintenance. Accumulation of 2',3'-cAMP is found in very young CNPase-deficient mice used to study traumatic brain injury, which develops post-traumatic axonal degeneration similar to that of older CNPase-deficient mice that do not experience brain trauma
physiological function
-
the enzyme encoding gene may play an important role as a putative anti-inflammatory gene both in normal and injured brain
physiological function
-
the enzyme encoding gene may play an important role as a putative anti-inflammatory gene both in normal and injured brain
physiological function
-
the enzyme interacts with membrane surfaces, cytoskeletal proteins, and calmodulin
physiological function
-
the enzyme is involved in regulation of the nonspecific pore, addition of myelin fraction associated with brain mitochondria to the suspension of liver mitochondria can lead to binding of the enzyme and myelin basic protein, present in the fraction with liver mitochondria under the conditions of both closed and opened permeability transition pore
physiological function
-
the enzyme is possible auto-antigen in multiple sclerosis. CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C. The mitochondrial, fully-processed isoform II does not drive morphological differentiation in cell cultures as isoform I does in oligodendrocytes. The enzyme, together with 2',3'-cAMP, is suggested to modulate the mitochondrial permeability transition, a proapoptotic event, in which Ca2+ is released from the mitochondrial matrix to the intermembrane space and cytoplasm
physiological function
the enzyme might be a mediator of interferon-induced response against hepatitis B virus. Isozymes CNP1 and CNP2 potently inhibit hepatitis B virus production by blocking viral proteins synthesis and reducing viral RNAs, respectively. Inhibition by isozymes CNP1 and CNP2 appear to have distinct mechanism. In chronic hepatitis B patients, the enzyme is expressed in most of hepatitis B virus -infected hepatocytes of liver specimens. Because the enzyme targets the poly(A) of mRNA, it exhibited a nonspecific effect on protein synthesis
physiological function
melatonin retains the enzyme inside mitochondria, thereby providing the protection of the protein against deleterious effects of 2',3'-cAMP in aging
physiological function
the enzyme interacts with microtubules and promotes tubulin polymerization
physiological function
the enzyme interacts with microtubules and promotes tubulin polymerization
physiological function
-
the enzyme encoding gene may play an important role as a putative anti-inflammatory gene both in normal and injured brain
-
physiological function
-
the enzyme is involved in regulation of the nonspecific pore, addition of myelin fraction associated with brain mitochondria to the suspension of liver mitochondria can lead to binding of the enzyme and myelin basic protein, present in the fraction with liver mitochondria under the conditions of both closed and opened permeability transition pore
-
physiological function
-
the enzyme encoding gene may play an important role as a putative anti-inflammatory gene both in normal and injured brain
-
additional information
binding mode of nucleotide ligands in the active site, structure-function analysis, catalytic mechanism, overview. Flexible loops might play roles in substrate recognition. The enzyme's N-terminal domain is involved in RNA binding and dimerization
additional information
-
binding mode of nucleotide ligands in the active site, structure-function analysis, catalytic mechanism, overview. Flexible loops might play roles in substrate recognition. The enzyme's N-terminal domain is involved in RNA binding and dimerization
additional information
-
role for the N-terminal domain of the enzyme in mediating multiple molecular interactions, molecular modeling, overview
additional information
-
role for the N-terminal domain of the enzyme in mediating multiple molecular interactions, molecular modeling, overview
additional information
-
structure of the 2'-cyclic AM-bound enzyme active site and its catalytic mechanism, overview
additional information
-
structure of the CNPase phosphodiesterase domain and its catalytic mechanism, overview
additional information
the enzyme shows an open/close motion of the beta5-alpha7 loop linked to the reaction. The two domains of the enzyme form an elongated molecule. The active site includes the two HxTx motifs on beta strands beta2 and beta5, between which lie four water molecules, forming the bottom of the active site. The N-terminus of helix alpha7, which is unique for the enzyme in the 2H family, plays a role during the reaction indicating that 2H phosphoesterases differ in their respective reaction mechanisms despite the conserved catalytic residues
additional information
-
the enzyme shows an open/close motion of the beta5-alpha7 loop linked to the reaction. The two domains of the enzyme form an elongated molecule. The active site includes the two HxTx motifs on beta strands beta2 and beta5, between which lie four water molecules, forming the bottom of the active site. The N-terminus of helix alpha7, which is unique for the enzyme in the 2H family, plays a role during the reaction indicating that 2H phosphoesterases differ in their respective reaction mechanisms despite the conserved catalytic residues
Show AA Sequence and Transmembrane Helices (1145 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
26700
-
x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase
31000
40000
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
45200
-
x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase
46000
48000
50000
additional information
-
in lipid raft fraction from an aged monkey, evidence of sequential CNP proteolysis, abundance of CNP immunoreactive higher molecular weight material
100000
-
sucrose density gradient centrifugation in the presence of bovine serum albumin or human gamma globulin or carbonic anhydrase or myelin basic protein
100000
-
gel filtration and gel electrophoresis under non reducing conditions, sucrose density gradient centrifugation
100000
-
gel filtration and gel electrophoresis under non reducing conditions, sucrose density gradient centrifugation
100000
-
gel filtration and gel electrophoresis under non reducing conditions, sucrose density gradient centrifugation
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
46000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
48000
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
50000
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
monomer or dimer
monomer-dimer equilibrium for full-length enzyme, dimerization is possibly mediated by the N-terminal domain
oligomer
additional information
?
-
x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
dimer
-
x * 48000, CNP2, x * 46000, CNP1, SDS-PAGE, under non-reducing conditions, composed of mixed subunits, ratio CNP2/CNP1 ranging from 2:1 in bovine to 1:10 in mouse and rat
additional information
-
enzyme interacts with tubulin, binding preferentially to tubulin heterodimers and inducing assembly of mircotubulues by cooperation with tubulin
additional information
the two domains of the enzyme form an elongated molecule, three-dimensional model of full-length enzyme, overveiw
additional information
-
the two domains of the enzyme form an elongated molecule, three-dimensional model of full-length enzyme, overveiw
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
a 13 residue C-terminal fragment is responsible for enzyme membrane anchoring. Lipidation of the 13 residue fragment is essential for the peptide to be folded and correctly positioned on the membrane surface
phosphoprotein
proteolytic modification
-
enzyme contains a mitochondrial targeting signal at the N-terminus. Import to mitochondria leads to cleavage of signal sequence yielding a mature, truncated form of CNP2 similar in size as CNP1. Phosphorylation of the signal sequence by protein kinase C inhibits translocation to mitochondria.
side-chain modification
phosphoprotein
-
CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C
phosphoprotein
-
both isoforms CNP1 and CNP2 are tyrosine-phosphorylated to a basal extend
phosphoprotein
-
CNP is phosphorylated in vivo by protein kinase C, phosphorylation of CNP1 interferes with its microtubule assembly-promoting activity
phosphoprotein
-
only CNP2 is phosphorylated in vivo, CNP1 not, Ser-9 of CNP2 is phosphorylated by a 4-beta-phorbol 12,13-dibutyrate-sensitive kinase, likely protein kinase C, and Ser-22 appears to be constitutively phosphorylated, phosphorylation of Ser-9 may provide a molecular switching mechanism for modulating the function of CNP2 distinguishing it functionally from CNP1
phosphoprotein
-
Ca2+-stimulated and permeability transition pore-associated enzyme phosphorylation on Ser and Thr residues. Permeability transition pore inducer Atr is able to stimulate the ATP incorporation into 46 kDa enzyme in the presence of threshold Ca2+, whereas CsA suppresses significantly phosphorylation of the enzyme
phosphoprotein
-
two phosphorylation sites on Tyr110 and Ser169 within the N-terminal domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain, sittging drop vapor diffusion method, using 20-35% (w/v) PEG3350, PEG4000, or PEG6000 as precipitants and 50 mM Na acetate or 100 mM Na citrate, pH 3.0-5.0
phosphodiesterase domain of the enzyme with bound citrate, sulfate, NADP+, and 2-AMP, mixing of protein in 10 mM sodium citrate pH 5.5, 50 mM NaCl, 10% glycerol, and 1 mM DTT, with crystallization solution, X-ray diffraction structure determination and analysis at 1.74-2.4 A resolution, molecular replacement and modeling. Crystallization is only successful with sulfate or citrate present
wild-type and mutant enzymes complexed with substrate 2',3'-cyclic AMP, product 2'-AMP, and phosphorothioate analogues, and H230S mutant complexed with the substrate 2',3'-cNADP+, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
modeling of enzyme N-terminal region and simulation of docking of nucleotides
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H189A
-
slight increase of Km value with 6fold decrease in kcat value
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
H225A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
H305A
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
H230Q
H230Q/H309Q
H230S
H309Q
H309S
P225G
the mutant shows increased activity compared to the wild type enzyme
P296G
the mutant shows slightly increased activity compared to the wild type enzyme
V321A
H230F
-
almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H230L
-
almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H309F
-
almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
H309L
-
almost inactive CNP1 catalytic fragment mutant with 1000fold lower kcat-value and similar Km-value compared with wild-type CNP1
additional information
H230Q
site-directed mutagenesis, the mutation of the active site residue highly reduces the enzyme activity compared to the wild-type enzyme
H230Q/H309Q
site-directed mutagenesis, the mutation of the active site residue completely abolishes enzyme activity compared to the wild-type enzyme
H230S
site-directed mutagenesis, the mutation of the active site residue highly reduces enzyme activity compared to the wild-type enzyme
H309Q
site-directed mutagenesis, the mutation of the active site residue highly reduces enzyme activity compared to the wild-type enzyme
H309S
the mutant shows strongly reduced activity compared to the wild type enzyme
H309S
site-directed mutagenesis, the mutation of the active site residue completely abolishes enzyme activity compared to the wild-type enzyme
V321A
site-directed mutagenesis, Val321 stacks against the substrate adenine ring, the mutation does not affect kcat significantly but doubles Km, indicating a functional active site but slightly compromised substrate binding
additional information
-
CNP1 promoter deletion and replacement mutants, effect on the stimulatory effect of cAMP on CNP1 gene expression
additional information
-
enzyme overexpression induces dramatic morphology changes in both glial and nonglial cells, resulting in microtubule and F-actin reorganization and formation of branched processes. Cultured oligodendrocytes from enzyme-deficient mice extend smaller outgrowths with less arborized processes
additional information
-
enzyme knockdown by siRNA knockdown of CNPase in BV-2 cells
additional information
-
C-terminal deletion of 13 amino acids of CNP1 leads to an abnormal microtubule distribution in the cell
additional information
-
CNP1: N-terminal deletion mutants, catalytic fragment corresponding to the last C-terminal 250 amino acids
additional information
-
expression of enzyme in yeast can complement growth of strains bearing lethal or temperature-sensitive mutations in the tRNA ligase 3'-end-healing domain
additional information
-
CNP-CF is a CNP1 deletion mutant lacking the first 150 amino acids
additional information
-
generation of inactive mutants truncated after amino acid 164
additional information
-
generation of truncated enzyme mutants: CNP_20-398, CNP_25-398, CNP_20-420, CNP_20-185, and CNP_179-398, analysis of calmodulin binding activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
in pH 5.5 and in the presence of 500 mM NaCl, CNPase is much more stable than at neutral pH with lower salt content
707896
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
80% loss of activity, and completely eliminated after 20 min, Co2+ protects against heat inactivation
65 - 75
-
increase in the melting temperature induced by both pH 5.5 and high salt concentration. At pH 5.5, without NaCl: ca. 68°C and with 500 mM NaCl: ca. 75°C. At pH 7.5 without NaCl and with 500 mM NaCl: ca. 70°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing, not affected by several cycles
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
at a final concentration up to 4% v/v of the total volume, no effect on CNP1 activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
4°C, Tris-acetate buffer, 0.5 mM dithiothreitol, pH 7.6, 10% glycerol, protease inhibitor mix, 3 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, by delipidation, solubilization, gel chromatography, resolubilization, ion-exchange chromatography and affinity chromatography
-
recombinant His-tagged wild-type full-length enzyme and truncated mutants by nickel affinity chromatography and gel filtration or by calmodulin affinity chromatography
-
recombinant tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CNP gene with various deletions of the CNP promoter, expression in rat C6 cells, regulation of CNP1 promoter activity by cAMP
-
full-length CNP1 and C-terminal deletion mutant, fused to glutathione S-transferase, expression in Escherichia coli JM83, fused to green fluorescent protein, expression in COS-7 cells
-
GC-CNP encoding 155238 aa of GFP fused to the N-terminus of CNP co-transfected with YN-Ub into COS-7 cells
-
GC-CNP encoding 155238 aa of GFP fused to the N-terminus of CNP co-transfected with YN-Ub into MO3.13 cells
-
gene CNP1, two isozymes, which originate from two alternative promoters and 3',5'-cAMP-regulated splicing of one of the mRNA variants produced from the CNP1 gene on chromosome 17
-
overexpression in Rattus norvegicus preglomerular vascular smooth muscle cells increasing the metabolism of exogenous 2,3'-cAMP to 2'-AMP
-
recombinant expression of His-tagged wild-type full-length enzyme and truncated mutants
-
subcloned into pTH27, expressed in Escherichia coli Rosetta (DE3) with a TEV protease-cleavable His-tag
-
tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
wild type and mutant CNP proteins are produced in vitro in rabbit reticulocyte lysate in the presence of S-methionine
-
wild-type and mutant CNP2, expression in 293T human kidney fibroblast cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after treatment with a single dose of aniline at 1000 mg/kg, expression of CNPase increases from day 2 and peaks on days 3 and 4
-
after treatment with a single dose of aniline at 1000 mg/kg, spongy change in the spinal cord from day 5, after which CNPase expression decreases remarkably
-
enzyme expression is upregulated in activated microglia as a response to brain injury
expression of CNP is reduced by 10% in schizophrenics compared with controls, but the difference is not significant
-
markedly enhanced enzyme expression, CNPase protein and mRNA expression, in microglia after activation by lipopolysaccharide treatment
treatment of purified adult canine olfactory ensheathing cells with fibroblast growth factor-2 significantly reduces CNPase expression at the protein and mRNA level
-
enzyme expression is upregulated in activated microglia as a response to brain injury
enzyme expression is upregulated in activated microglia as a response to brain injury
markedly enhanced enzyme expression, CNPase protein and mRNA expression, in microglia after activation by lipopolysaccharide treatment
-
markedly enhanced enzyme expression, CNPase protein and mRNA expression, in microglia after activation by lipopolysaccharide treatment
-
markedly enhanced enzyme expression, CNPase protein and mRNA expression, in microglia after activation by lipopolysaccharide treatment
-
-
markedly enhanced enzyme expression, CNPase protein and mRNA expression, in microglia after activation by lipopolysaccharide treatment
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
2',3'-cyclic nucleotide 3'-phosphodiesterase is a stable marker for in situ detection of canine but not rat olfactory ensheathing cells
diagnostics
-
2',3'-cyclic nucleotide 3'-phosphodiesterase is a stable marker for in situ detection of canine but not rat olfactory ensheathing cells
medicine
medicine
-
cells derived from transplanted marrow stromal cells can transform into cells resembling Schwann cells, whereas host-derived glial cells participate in formation of perineural compartments. The chemotactic migration of both host-derived and transplantation-derived cells bearing the enzyme in their plasma membrane may be attracted by stromal derived factor-1alpha produced locally
medicine
-
no association between genetic variation in the CNP enzyme gene and schizophrenia in the Han Chinese population
medicine
2',3'-cyclic nucleotide 3'-phosphodiesterase single nucleotide polymorphism rs2070106 is potentially associated with schizophrenia
medicine
the rs207016 genotype of CNP is not likely to contribute to the coordinated down-regulation of oligodendrococyte-related genes in schizophrenia
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Helfman, D.M.; Shoji, M.; Kuo, J.F.
Purification to homogeneity and general properties of a novel phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP
J. Biol. Chem.
256
6327-6334
1981
Sus scrofa
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Sprinkle, T.J.
2'3'-cyclic nucleotide 3'-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system
CRC Crit. Rev. Clin. Neurobiol.
4
235-301
1989
Bos taurus, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Oryctolagus cuniculus, Chondrichthyes, Haemophilus influenzae, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa, Xenopus laevis
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Vogel, U.S.; Thompson, R.J.
Molecular structure, localization, and possible functions of the myelin-associated enzyme 2,3-cyclic nucleotide 3-phosphodiesterase
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50
1667-1677
1988
Bos taurus, Chondrichthyes, Gallus gallus, Homo sapiens, Rattus norvegicus, Xenopus laevis
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Sims, N.R.; Carnegie, P.R.
2'3'-cyclic nucleotide 3'-phosphodiesterase
Adv. Neurochem.
3
1-41
1978
Bos taurus, Canis lupus familiaris
-
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Tsukada, Y.; Suda, H.
Solubilization and purification of 2,3-cyclic nucleotide 3-phosphohydrolase (CNP-A) from bovine cerebral white matter-a review
Cell. Mol. Biol.
26
493-504
1980
Bos taurus
brenda
Kurihara, T.; Fowler, A.V.; Takahshi, Y.
cDNA cloning and amino acid sequence of bovine brain 2,3-cyclic-nucleotide 3-phosphodiesterase [published erratum appears in J. Biol. Chem. 1987 Dec 5; 262(34):16754]
J. Biol. Chem.
262
3256-3261
1987
Bos taurus
brenda
Vogel, U.S.; Thompson, R.J.
Molecular cloning of the myelin specific enzyme 2,3-cyclic-nucleotide 3-phosphohydrolase
FEBS Lett.
218
261-265
1987
Bos taurus
brenda
Kurihara, T.; Takahshi, Y.; Nishiyama, A.; Kumanishi, T.
cDNA cloning and amino acid sequence of human brain 2,3-cyclic-nucleotide 3-phosphodiesterase
Biochem. Biophys. Res. Commun.
152
837-842
1988
Homo sapiens
brenda
Tyc, K.; Kellenberger, C.; Filipowicz, W.
Purification and characterization of wheat germ 2,3-cyclic nucleotide 3-phosphodiesterase
J. Biol. Chem.
262
12994-1300
1987
Triticum aestivum
brenda
Muller, H.W.; Clapshaw, P.A.; Seifert, W.
Two molecular forms of the isolated brain enzyme 2,3-cyclic nucleotide 3-phosphodiesterase
FEBS Lett.
131
37-40
1981
Bos taurus
brenda
Kurihara, T.; Nishizawa, Y.; Takahshi, Y.; Odani, S.
Chemical, immunological and catalytic properties of 2:3-cyclic nucleotide 3-phosphodiesterase purified from brain white matter
Biochem. J.
195
153-157
1981
Bos taurus
brenda
Nishizawa, Y.; Kurihara, T.; Takahshi, T.
Spectrophotometric assay, solubilization and purification of brain 2':3'-cyclic nucleotide 3-phosphodiesterase
Biochem. J.
191
71-82
1980
Bos taurus
brenda
Sprinkle, T.J.; Tippins, R.B.; Kestler, D.P.
Inhibition of bovine and human brain 2':3'-cyclic nucleotide 3-phosphodiesterase by heparin and polyribonucleotides and evidence for an associated 5-polynucleotide kinase activity
Biochem. Biophys. Res. Commun.
145
686-691
1987
Bos taurus, Homo sapiens
brenda
Carey, E.M.; Reynolds, R.; Herschkowitz, N.
Expression of 2'3'-cyclic nucleotide 3'-phosphohydrolase and myelin basic protein, and formation of oligodendrocytes in mixed glial cultures maintained in a defined medium
Biochem. Soc. Trans.
16
900-901
1988
Mus musculus
-
brenda
Bassett, J.H.D.; Vogel, U.S.; Thompson, R.J.
Molecular analysis of human 2',3'-cyclic nucleotide 3'-phosphohydrolase
Biochem. Soc. Trans.
16
304-305
1988
Homo sapiens
-
brenda
Jones, M.; Keenan, R.W.
Specific localization of 2,3-cyclic nucleotide 3-phosphohydrolase, (Ca2+/Mg2+)-ATPase, and acetylcholinesterase in human erythrocyte membrane
Biochim. Biophys. Acta
678
403-407
1981
Homo sapiens
brenda
Dreiling, C.E.
Localization of 2,3-cyclic nucleotide 3-phosphodiesterase in human erythrocyte membranes
Biochim. Biophys. Acta
649
587-594
1981
Homo sapiens
brenda
Dreiling, C.E.; Schilling, R.J.; Reitz, R.C.
2,3-cyclic nucleotide 3-phosphohydrolase in rat liver mitochondrial membranes
Biochim. Biophys. Acta
640
114-120
1981
Rattus norvegicus
brenda
Giulian, D.; Moore, S.
Identification of 2:3-cyclic nucleotide 3-phosphodiesterase in the vertebrate retina
J. Biol. Chem.
255
5993-5995
1980
Bos taurus, Carassius auratus
brenda
Holy, A.; Rosenberg, I.
New pyrimidine (uridine) specific cyclizing 2'-ribonucleotidyltransferase and nonspecific decyclizing 2',3'-phosphodiesterase
Collect. Czech. Chem. Commun.
44
957-975
1979
Brassica napus
-
brenda
Lin, L.F.H.; Bartlett, C.; Lees, M.B.
Preparation and characterization of unilamellar myelin vesicles
J. Biol. Chem.
261
16241-16246
1986
Rattus norvegicus
brenda
Drummond, G.I.; Iyer, N.T.; Keith, J.
Hydrolysis of ribonucleoside 2',3'-cyclic phosphates by a diesterase from brain
J. Biol. Chem.
237
3535-3539
1962
Bos taurus
-
brenda
Blair, G.E.; Sawecka, J.; Griffiths, S.A.; Blair Zajdel, M.E.
Biosynthesis of 2',3'-cyclic nucleotide 3'-phosphodiesterase (Wolfgram proteins) in rat brain and glioma cells
Biochem. Soc. Trans.
16
212-213
1988
Rattus norvegicus
-
brenda
Foster, P.C.; Carey, E.M.
2':3'-cyclic nucleotide 3-phosphohydrolase activity in human infant corpus callosum
Biochem. Soc. Trans.
8
610-611
1980
Homo sapiens
brenda
Sudo, T.; Kikuno, M.; Kurihara, T.
2',3'-cyclic nucleotide 3-phosphohydrolase in human erythrocyte membranes
Biochim. Biophys. Acta
255
640-646
1972
Homo sapiens
brenda
Prohaska, J.R.; Clark, D.A.; Wells, W.W.
Improved rapidity and precision in the determination of brain 2',3'-cyclic nucleotide 3-phosphohydrolase
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56
275-282
1973
Gallus gallus, Mus musculus, Rattus norvegicus
brenda
Seki, T.; Fukuda, S.
Purification and some properties of 2',3'-cyclic phosphodiesterase from the cell-free extract of Bacillus subtilis var. amyloliquefacus
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27
487-498
1981
Bacillus subtilis
-
brenda
Helfman, D.M.; Kuo, J.F.
A homogenous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2':3'- and 3':5'- nucleotides
J. Biol. Chem.
257
1044-1047
1982
Sus scrofa
brenda
Waehneldt, T.V.
Ontogenetic study of a myelin-derived fraction with 2':3'-cyclic nucleotide 3'-phosphohydrolase activity higher than that of myelin
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151
435-437
1975
Rattus norvegicus
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Effects of chronic ethanol ingestion on the activity of rat liver mitochondrial 2',3'- cyclic nucleotide
Biochim. Biophys. Acta
640
121-130
1981
Rattus norvegicus
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Mammalian membrane marker enzymes: sensitive assay for 5'-nucleotidase and assay for mammalian 2',3'-cyclic-nucleotide-3'-phosphohydrolase
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32
124-131
1974
Mammalia
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Thompson, W.J.; Brooker, G.; Appleman, M.M.
Assay of cyclic nucleotide phosphodiesterases with radioactive substrates
Methods Enzymol.
38C
205-212
1974
Ophiophagus hannah
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Lin, Y.M.; Liu, Y.P.; Cheung, W.Y.
Purification and characterization of a protein activator of cyclic nucleotide phosphodiesterase from bovine brain
Methods Enzymol.
38C
262-273
1974
Bos taurus
-
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Brown, E.G.; Edwards, M.J.; Newton, R.P.; Smith, C.J.
The cyclic nucleotide phosphodiesterases of spinach chloroplasts and microsomes
Phytochemistry
19
23-30
1980
Spinacia oleracea
-
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Craven, P.A.; Neidig, M.; De Rubertis, F.R.
Properties of multiple kinetic forms of soluble cyclic nucleotide phosphodiesterase activity of rat colonic mucosa
Biochim. Biophys. Acta
744
265-275
1983
Rattus norvegicus
brenda
Diaz, A.R.; Heredia, C.F.
Purification and characterization of Artemia 2',3'- cyclic nucleotide 3'-phosphodiesterase
Biochim. Biophys. Acta
1290
135-140
1996
Artemia sp.
brenda
Genschik, P.; Hall, J.; Filipowicz, W.
Cloning and characterization of the Arabidopsis cyclic phosphodiesterase which hydrolyzes ADP-ribose 1'',2''-cyclic phosphate and nucleoside 2',3'-cyclic phophates
J. Biol. Chem.
272
13211-13219
1997
Arabidopsis thaliana
brenda
Ballestero, R.P.; Dybowski, J.A.; Levy, G.; Agranoff, B.W.; Uhler M.D.
Cloning and characterization of zRich, a 2',3'-cyclic-nucleotide 3'- phosphodiesterase induced during zebrafish optic nerve regeneration
J. Neurochem.
72
1362-1371
1999
Danio rerio
brenda
Stricker, R.; Lottspeich, F.; Reiser, G.
The myelin protein CNP (2',3'-cyclic nucleotide 3'-phosphodiesterase): Immunoaffinity purification of CNP from pig and rat brain using a monoclonal antibody and phosphorylation of CNP by cyclic nucleotide-dependent protein kinases
Biol. Chem. Hoppe-Seyler
375
205-209
1994
Rattus norvegicus, Sus scrofa
brenda
Fressinaud, C.; Sarlieve, L.L.; Dalencon, D.; Labourdette, G.
Differential regulation of cerebroside sulfotransferase and 2',3'-cyclic nucleotide 3'-phosphodiesterase by basic fibroblast growth factor in relation to proliferation in rat oligodendrocyte cultures
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150
34-44
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Rattus norvegicus
brenda
Braun, P.E.; Bambrick, L.L.; Edwards, A.M.; Bernier, L.
2',3'-cyclic-nucleotide 3'- phosphodiesterase has characteristics of cytoskeletal proteins. A hypothesis for its function
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605
55-65
1990
Bos taurus, Rattus norvegicus
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Kasama, H.Y.; Tohyama, Y.; Kurihara, T.; Sakuma, M.; Kojima, H.; Tamai, Y.
A comparative study of 2',3'-cyclic nucleotide 3'-phosphodiesterase in vertebrates: cDNA cloning and amino acid sequences for chicken and bullfrog enzymes
J. Neurochem.
69
1335-1342
1997
Gallus gallus, Lithobates catesbeianus
brenda
Gravel, M.; DeAngelis, D.; Braun, P.E.
Molecular cloning and characterization of rat brain 2',3'-phosphodiesterase isoform 2
J. Neurosci. Res.
38
243-247
1994
Rattus norvegicus
brenda
Yin, X.; Peterson, J.; Gravel, M.; Braun, P.E.; Trapp, B.D.
CNP overexpression induces aberrant oligodendrocyte membranes and inhibits MBP accumulation and myelin compaction
J. Neurosci. Res.
50
238-247
1997
Homo sapiens
brenda
Barradas, P.C.; Gomes, S.S.; Cavalcante, L.A.
CNPase expression in the developing opossum brain stem and cerebellum
Neuroreport
6
289-292
1995
Didelphidae
brenda
Stephon, R.L.; Niedbala, R.S.; Schray, K.J.; Heindel, N.D.
An enzymatic cycling procedure for beta-NADP+ generated by 3'-phosphdiesterase, 2':3'-cyclic nucleotide
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202
6-9
1992
Homo sapiens
brenda
Bichenkov, E.; Ellingson, J.S.
Ethanol exerts different effects on myelin basic protein and 2',3'-cyclic nucleotide 3'-phosphodiesterase expression in differentiating CG-4 oligodendrocytes
Brain Res. Dev. Brain Res.
128
9-16
2001
Rattus norvegicus
brenda
Barradas, P.C.; Ferraz, A.S.; Ferreira, A.A.; Daumas, R.P.; Moura, E.G.
2'3'Cyclic nucleotide 3'phosphodiesterase immunohistochemistry shows an impairment on myelin compaction in hypothyroid rats
Int. J. Dev. Neurosci.
18
887-892
2000
Rattus norvegicus
brenda
Lee, J.; Gravel, M.; Gao, E.; O'Neill, R.C.; Braun, P.E.
Identification of essential residues in 2',3'-cyclic nucleotide 3'-phosphodiesterase. Chemical modification and site-directed mutagenesis to investigate the role of cysteine and histidine residues in enzymatic activity
J. Biol. Chem.
276
14804-14813
2001
Rattus norvegicus
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, Escherichia coli (P06961)
brenda
O'Neill, R.C.; Braun, P.E.
Selective synthesis of 2',3'-cyclic nucleotide 3'-phosphodiesterase isoform 2 and identification of specifically phosphorylated serine residues
J. Neurochem.
74
540-546
2000
Rattus norvegicus
brenda
Gravel, M.; Gao, E.; Hervouet-Zeiber, C.; Parsons, V.; Braun, P.E.
Transcriptional regulation of 2',3'-cyclic nucleotide 3'-phosphodiesterase gene expression by cyclic AMP in C6 cells
J. Neurochem.
75
1940-1950
2000
Mus musculus, Rattus norvegicus
brenda
Gomes, S.S.; Carvalho, S.L.; Santiago, M.F.; Lopez, L.B.; Barradas, P.C.; Cavalcante, L.A.
Expression of 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) in the developing olfactory bulb and subventricular zone rostral extension
J. Neurosci. Res.
73
471-480
2003
Rattus norvegicus
brenda
Cho, S.J.; Jung, J.S.; Jin, I.; Moon, I.S.
2', 3'-cyclic nucleotide 3'-phosphodiesterase is expressed in dissociated rat cerebellar cells and included in the postsynaptic density fraction
Mol. Cells
16
128-135
2003
Rattus norvegicus
brenda
Santos-Silva, A.; Cavalcante, L.A.
Expression of the non-compact myelin protein 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) in olfactory bulb ensheathing glia from explant cultures
Neurosci. Res.
40
189-193
2001
Rattus norvegicus
brenda
Bifulco, M.; Laezza, C.; Stingo, S.; Wolff, J.
2',3'-Cyclic nucleotide 3'-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin
Proc. Natl. Acad. Sci. USA
99
1807-1812
2002
Rattus norvegicus
brenda
Sakamoto, Y.; Tanaka, N.; Ichimiya, T.; Kurihara, T.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic studies of human 2',3'-cyclic nucleotide 3'-phosphodiesterase
Acta Crystallogr. Sect. D
60
2095-2097
2004
Homo sapiens
brenda
Dabrowska-Bouta, B.; Sulkowski, G.; Struzynska, L.; Rafalowska, U.
CNPase activity in myelin from adult rat brains after prolonged lead exposure in vivo
Chem. Biol. Interact.
150
171-178
2004
Rattus norvegicus
brenda
Lee, J.; Gravel, M.; Zhang, R.; Thibault, P.; Braun, P.E.
Process outgrowth in oligodendrocytes is mediated by CNP, a novel microtubule assembly myelin protein
J. Cell Biol.
170
661-673
2005
Mus musculus
brenda
Sakamoto, Y.; Tanaka, N.; Ichimiya, T.; Kurihara, T.; Nakamura, K.T.
Crystal structure of the catalytic fragment of human brain 2',3'-cyclic-nucleotide 3'-phosphodiesterase
J. Mol. Biol.
346
789-800
2005
Homo sapiens
brenda
Lee, J.; O'Neill, R.C.; Park, M.W.; Gravel, M.; Braun, P.E.
Mitochondrial localization of CNP2 is regulated by phosphorylation of the N-terminal targeting signal by PKC: implications of a mitochondrial function for CNP2 in glial and non-glial cells
Mol. Cell. Neurosci.
31
446-462
2006
Rattus norvegicus
brenda
Zhang, B.; Cao, Q.; Guo, A.; Chu, H.; Chan, Y.G.; Buschdorf, J.P.; Low, B.C.; Ling, E.A.; Liang, F.
Juxtanodin: an oligodendroglial protein that promotes cellular arborization and 2',3'-cyclic nucleotide-3'-phosphodiesterase trafficking
Proc. Natl. Acad. Sci. USA
102
11527-11532
2005
Rattus norvegicus
brenda
Esposito, C.; Scrima, M.; Carotenuto, A.; Tedeschi, A.; Rovero, P.; DErrico, G.; Malfitano, A.M.; Bifulco, M.; DUrsi, A.M.
Structures and micelle locations of the nonlipidated and lipidated C-terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase
Biochemistry
47
308-319
2008
Rattus norvegicus
brenda
Stingo, S.; Masullo, M.; Polverini, E.; Laezza, C.; Ruggiero, I.; Arcone, R.; Ruozi, E.; Dal Piaz, F.; Malfitano, A.M.; DUrsi, A.M.; Bifulco, M.
The N-terminal domain of 2,3-cyclic nucleotide 3-phosphodiesterase harbors a GTP/ATP binding site
Chem. Biol. Drug Des.
70
502-510
2007
Rattus norvegicus
brenda
Cao, Q.; Ding, P.; Lu, J.; Dheen, S.T.; Moochhala, S.; Ling, E.A.
2',3'-Cyclic nucleotide 3'-phosphodiesterase cells derived from transplanted marrow stromal cells and host tissue contribute to perineurial compartment formation in injured rat spinal cord
J. Neurosci. Res.
85
116-130
2007
Rattus norvegicus
brenda
Tang, F.; Qu, M.; Wang, L.; Ruan, Y.; Lu, T.; Zhang, H.; Liu, Z.; Yue, W.; Zhang, D.
Case-control association study of the 2,3-cyclic nucleotide 3-phosphodiesterase (CNP) gene and schizophrenia in the Han Chinese population
Neurosci. Lett.
416
113-116
2007
Homo sapiens
brenda
Wu, C.Y.; Lu, J.; Cao, Q.; Guo, C.H.; Gao, Q.; Ling, E.A.
Expression of 2,3-cyclic nucleotide 3-phosphodiesterase in the amoeboid microglial cells in the developing rat brain
Neuroscience
142
333-341
2006
Rattus norvegicus
brenda
Keppetipola, N.; Shuman, S.
Characterization of the 2,3 cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase
Nucleic Acids Res.
35
7721-7732
2007
Acetivibrio thermocellus
brenda
Schwer, B.; Aronova, A.; Ramirez, A.; Braun, P.; Shuman, S.
Mammalian 2,3 cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo
RNA
14
204-210
2008
Rattus norvegicus
brenda
Gravel, M.; Robert, F.; Kottis, V.; Gallouzi, I.E.; Pelletier, J.; Braun, P.E.
2,3-Cyclic nucleotide 3-phosphodiesterase: a novel RNA-binding protein that inhibits protein synthesis
J. Neurosci. Res.
87
1069-1079
2009
Rattus norvegicus
brenda
Lovato, L.; Cianti, R.; Gini, B.; Marconi, S.; Bianchi, L.; Armini, A.; Anghileri, E.; Locatelli, F.; Paoletti, F.; Franciotta, D.; Bini, L.; Bonetti, B.
Transketolase and CNPase I are specifically recognized by IgG autoantibodies in multiple sclerosis patients
Mol. Cell. Proteomics
7
2337-2349
2008
Homo sapiens (P09543), Homo sapiens
brenda
Voineskos, A.N.; de Luca, V.; Bulgin, N.L.; van Adrichem, Q.; Shaikh, S.; Lang, D.J.; Honer, W.G.; Kennedy, J.L.
A family-based association study of the myelin-associated glycoprotein and 2',3'-cyclic nucleotide 3'-phosphodiesterase genes with schizophrenia
Psychiatr. Genet.
18
143-146
2008
Homo sapiens (P09543)
brenda
Iwamoto, K.; Ueda, J.; Bundo, M.; Nakano, Y.; Kato, T.
Effect of a functional single nucleotide polymorphism in the 2',3'-cyclic nucleotide 3'-phosphodiesterase gene on the expression of oligodendrocyte-related genes in schizophrenia
Psychiatry Clin. Neurosci.
62
103-108
2008
Homo sapiens (P09543), Homo sapiens
brenda
Che, R.; Tang, W.; Zhang, J.; Wei, Z.; Zhang, Z.; Huang, K.; Zhao, X.; Gao, J.; Zhou, G.; Huang, P.; He, L.; Shi, Y.
No relationship between 2',3'-cyclic nucleotide 3'-phosphodiesterase and schizophrenia in the Chinese Han population: an expression study and meta-analysis
BMC Med. Genet.
10
31
2009
Homo sapiens
brenda
Myllykoski, M.; Kursula, P.
Expression, purification, and initial characterization of different domains of recombinant mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase, an enigmatic enzyme from the myelin sheath
BMC Res. Notes
3
12
2010
Mus musculus
brenda
Hinman, J.; Chen, C.; Oh, S.; Hollander, W.; Abraham, C.
Age-dependent accumulation of ubiquitinated 2',3'-cyclic nucleotide 3'-phosphodiesterase in myelin lipid rafts
Glia
56
118-133
2008
Chlorocebus aethiops, Homo sapiens, Macaca mulatta
brenda
Kanno, T.; Kurotaki, T.; Yamada, N.; Yamashita, K.; Wako, Y.; Tsuchitani, M.
Activity of 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) in spinal cord with spongy change induced by a single oral dose of aniline in rats
Toxicol. Pathol.
38
359-365
2010
Rattus norvegicus
brenda
Sumiyoshi, K.; Obayashi, S.; Tabunoki, H.; Arima, K.; Satoh, J.
Protein microarray analysis identifies cyclic nucleotide phosphodiesterase as an interactor of Nogo-A
Neuropathology
30
7-14
2010
Homo sapiens
brenda
Rao, F.; Qi, Y.; Murugan, E.; Pasunooti, S.; Ji, Q.
2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: implications for PDE screening
Biochem. Biophys. Res. Commun.
398
500-505
2010
Rattus norvegicus
brenda
Omar, M.; Bock, P.; Kreutzer, R.; Ziege, S.; Imbschweiler, I.; Hansmann, F.; Peck, C.T.; Baumgaertner, W.; Wewetzer, K.
Defining the morphological phenotype: 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) is a novel marker for in situ detection of canine but not rat olfactory ensheathing cells
Cell Tissue Res.
344
391-405
2011
Canis lupus familiaris, no activity in Rattus norvegicus
brenda
Nielsen, A.B.; Jensen, H.E.; Leifsson, P.S.
Immunohistochemistry for 2',3'-cyclic nucleotide-3-phosphohydrolase in 63 bovine peripheral nerve sheath tumors
Vet. Pathol.
48
796-802
2011
Bos taurus
brenda
Jackson, E.K.; Gillespie, D.G.; Mi, Z.; Cheng, D.; Bansal, R.; Janesko-Feldman, K.; Kochanek, P.M.
Role of 2',3'-cyclic nucleotide 3'-phosphodiesterase in the renal 2',3'-cAMP-adenosine pathway
Am. J. Physiol. Renal Physiol.
307
F14-F24
2014
Homo sapiens
brenda
Baburina, Y.L.; Gordeeva, A.E.; Moshkov, D.A.; Krestinina, O.V.; Azarashvili, A.A.; Odinokova, I.V.; Azarashvili, T.S.
Interaction of myelin basic protein and 2',3'-cyclic nucleotide phosphodiesterase with mitochondria
Biochemistry (Moscow)
79
555-565
2014
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Azarashvili, T.; Krestinina, O.; Galvita, A.; Grachev, D.; Baburina, Y.; Stricker, R.; Reiser, G.
Identification of phosphorylated form of 2, 3-cyclic nucleotide 3-phosphodiesterase (CNPase) as 46kDa phosphoprotein in brain non-synaptic mitochondria overloaded by calcium
J. Bioenerg. Biomembr.
46
135-145
2014
Rattus norvegicus
brenda
Myllykoski, M.; Raasakka, A.; Lehtimaeki, M.; Han, H.; Kursula, I.; Kursula, P.
Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family
J. Mol. Biol.
425
4307-4322
2013
Mus musculus (P16330), Mus musculus
brenda
Myllykoski, M.; Itoh, K.; Kangas, S.M.; Heape, A.M.; Kang, S.U.; Lubec, G.; Kursula, I.; Kursula, P.
The N-terminal domain of the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: direct molecular interaction with the calcium sensor calmodulin
J. Neurochem.
123
515-524
2012
Mus musculus, Rattus norvegicus
brenda
Yang, L.; Kan, E.M.; Lu, J.; Wu, C.; Ling, E.A.
Expression of 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) and its roles in activated microglia in vivo and in vitro
J. Neuroinflammation
11
148
2014
Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
brenda
Raasakka, A.; Kursula, P.
The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and function
Neurosci. Bull.
30
956-966
2014
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Myllykoski, M.; Raasakka, A.; Han, H.; Kursula, P.
Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation
PLoS ONE
7
e32336
2012
Mus musculus (P16330), Mus musculus
brenda
Ma, H.; Zhao, X.L.; Wang, X.Y.; Xie, X.W.; Han, J.C.; Guan, W.L.; Wang, Q.; Zhu, L.; Pan, X.B.; Wei, L.
2',3'-cyclic nucleotide 3'-phosphodiesterases inhibit hepatitis B virus replication
PLoS ONE
8
e80769
2013
Homo sapiens (P09543), Homo sapiens
brenda
Jackson, E.K.; Mi, Z.; Janesko-Feldman, K.; Jackson, T.C.; Kochanek, P.M.
2',3'-cGMP exists in vivo and comprises a 2',3'-cGMP-guanosine pathway
Am. J. Physiol. Regul. Integr. Comp. Physiol.
316
R783-R790
2019
Mus musculus
brenda
Baburina, Y.; Odinokova, I.; Azarashvili, T.; Akatov, V.; Lemasters, J.J.; Krestinina, O.
2',3'-Cyclic nucleotide 3'-phosphodiesterase as a messenger of protection of the mitochondrial function during melatonin treatment in aging
Biochim. Biophys. Acta
1859
94-103
2017
Rattus norvegicus (P13233)
brenda
Myllykoski, M.; Seidel, L.; Muruganandam, G.; Raasakka, A.; Torda, A.E.; Kursula, P.
Structural and functional evolution of 2',3'-cyclic nucleotide 3'-phosphodiesterase
Brain Res.
1641
64-78
2016
Rattus norvegicus (P13233), Mus musculus (P16330)
brenda
Baburina, Y.; Odinokova, I.; Azarashvili, T.; Akatov, V.; Sotnikova, L.; Krestinina, O.
Possible involvement of 2',3'-cyclic nucleotide-3'-phosphodiesterase in the protein phosphorylation-mediated regulation of the permeability transition pore
Int. J. Mol. Sci.
19
E3499
2018
Rattus norvegicus
brenda
Jackson, E.K.; Menshikova, E.V.; Mi, Z.; Verrier, J.D.; Bansal, R.; Janesko-Feldman, K.; Jackson, T.C.; Kochanek, P.M.
Renal 2',3'-cyclic nucleotide 3'-phosphodiesterase is an important determinant of AKI severity after ischemia-reperfusion
J. Am. Soc. Nephrol.
27
2069-2081
2016
Mus musculus
brenda
Verrier, J.D.; Kochanek, P.M.; Jackson, E.K.
Schwann cells metabolize extracellular 2',3'-cAMP to 2'-AMP
J. Pharmacol. Exp. Ther.
354
175-183
2015
Rattus norvegicus
brenda
Baburina, Y.; Azarashvili, T.; Grachev, D.; Krestinina, O.; Galvita, A.; Stricker, R.; Reiser, G.
Mitochondrial 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) interacts with mPTP modulators and functional complexes (I-V) coupled with release of apoptotic factors
Neurochem. Int.
90
46-55
2015
Rattus norvegicus
brenda
Raasakka, A.; Myllykoski, M.; Laulumaa, S.; Lehtimaeki, M.; Haertlein, M.; Moulin, M.; Kursula, I.; Kursula, P.
Determinants of ligand binding and catalytic activity in the myelin enzyme 2,3-cyclic nucleotide 3-phosphodiesterase
Sci. Rep.
5
16520
2015
Mus musculus (P16330)
brenda
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