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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
- nervous
- mbp
- matter
- astrocyte
-
proteolipid
- oligodendroglial
-
axon
- glycoprotein
- nerve
- cord
- sheath
- cerebral
- sclerosis
-
myelin-associated
-
fibrillary
-
schwann
- callosum
-
corpus
- neurofilament
- galactocerebroside
-
myelin-related
-
3\'-cyclic
-
myelinogenesis
-
hypomyelination
-
remyelination
- sulfatide
-
sciatic
-
myelin-specific
- 5'-nucleotidase
- encephalomyelitis
- nestin
-
jimpy
-
dysmyelination
-
myelin-like
-
myelin-forming
-
ensheathing
-
quaking
- cuprizone
- medicine
- galactolipids
-
gfap-positive
- analysis
-
shiverer
- diagnostics
- cerebroside
-
luxol
-
paranodal
-
oligodendrocyte-specific
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
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'-cyclic nucleotide-3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphohydrolase, 2',3'-cyclic phosphodiesterase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase type I, 
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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
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
-
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
catalytic mechanism
-
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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
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
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
-
-
-
-
?
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
P13233
-
-
-
?
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+
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
Ca2+
-
Ca2+-stimulated and permeability transition pore-associated enzyme phosphorylation
Mg2+
activataes with 2'-AMP, KD: 0.24 +/- 0.1 mM; activates with 2',3'-cAMP, KD: 0.49 +/- 0.1 mM; activates with ATP, KD ~ 0.1 mM
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
18
cyclic 2',3'-AMP
-
mutant D236E, pH 7.5, 45°C; mutant D392E, pH 7.5, 45°C; wild-type, pH 7.5, 45°C
100
cyclic 2',3'-AMP
-
mutant D392A, pH 7.5, 45°C; mutant R237K, pH 7.5, 45°C
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
6.08
2',3'-cNADP
-
pH 6, 25°C, H230L mutant CNP1; pH 6, 25°C, H309L mutant CNP1
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; 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; 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; 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
-
135386, 135391, 135393, 135394, 135395, 135402, 135403, 135423, 135425, 667039, 669848, 682131, 707884, 708596, 713118, 728939
-
-
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, 750868, 751383, 751698
-
-
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
-
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
-
-
135380, 135381, 135399, 135401, 135404, 135407, 135418, 135419, 135422, 729185, 729954, 730238, 730475, 749958, 751698
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
-
the enzyme is one of the most abundant proteins in CNS myelin
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 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