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Information on EC 3.1.4.37 - 2',3'-cyclic-nucleotide 3'-phosphodiesterase and Organism(s) Homo sapiens and UniProt Accession P09543
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
cnpase, 2',3'-cyclic nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide 3'-phosphohydrolase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphodiesterase, 2',3'-cyclic nucleotide-3'-phosphohydrolase, 2':3'-cyclic nucleotide 3'-phosphodiesterase, 2',3'-cyclic nucleotide phosphodiesterase, 2',3'-cyclic-nucleotide 3'-phosphodiesterase type i, 2':3'-cnmp-3'-ase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2',3'-cyclic AMP phosphodiesterase
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2',3'-cyclic nucleoside monophosphate phosphodiesterase
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2',3'-cyclic nucleotide 3'-phosphodiesterase
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2',3'-cyclic nucleotide 3'-phosphohydrolase
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2',3'-cyclic nucleotide phosphohydrolase
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2':3'-cyclic nucleotide 3'-phosphodiesterase
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CNP
CNPase
cyclic 2',3'-nucleotide 3'-phosphodiesterase
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-
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cyclic 2',3'-nucleotide phosphodiesterase
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cyclic-CMP phosphodiesterase
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nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase
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phosphodiesterase, cyclic 2',3'-nucleotide 3'-
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CNP
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CNPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
general acid/general base catalysis by H310, H231 and a water molecule, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
nucleoside-2',3'-cyclic-phosphate 2'-nucleotidohydrolase
The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3',5'-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase.
CAS REGISTRY NUMBER
COMMENTARY
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
additional information
?
-
-
endogenous Nogo-A interacts with the endogenous CNP in vitro and in vivo
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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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
quantitative isozymes expression analysis in hepatoma cell lines
the enzyme is expressed in liver tissues with hepatitis B virus infection
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the enzyme is most abundant protein in non-compact myelin and the third-most abundant protein overall in CNS myellin
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the N-terminus ofisozyme CNP2 serves as a mitochondrial targeting signal and translocates it to the mitochondrion
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
knockdown of the enzyme expression moderately improves hepatitis B viral production in the HepG2.2.15 cells treated with IFN-alpha
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
evolution
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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
malfunction
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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
metabolism
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role of 2',3'-cyclic nucleotide 3'-phosphodiesterase in the renal 2',3'-cAMP-adenosine pathway, overview
physiological function
physiological function
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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
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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
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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
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CN37_HUMAN
421
0
47579
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
gel filtration and gel electrophoresis under non reducing conditions, sucrose density gradient centrifugation
46000
48000
46000
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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
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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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
GC-CNP encoding 155238 aa of GFP fused to the N-terminus of CNP co-transfected with YN-Ub into MO3.13 cells
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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
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overexpression in Rattus norvegicus preglomerular vascular smooth muscle cells increasing the metabolism of exogenous 2,3'-cAMP to 2'-AMP
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of CNP is reduced by 10% in schizophrenics compared with controls, but the difference is not significant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Vogel, U.S.; Thompson, R.J.
Molecular structure, localization, and possible functions of the myelin-associated enzyme 2,3-cyclic nucleotide 3-phosphodiesterase
J. Neurochem.
50
1667-1677
1988
Bos taurus, Gallus gallus, Chondrichthyes, Homo sapiens, Rattus norvegicus, Xenopus laevis
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
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
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
-
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
Dreiling, C.E.
Localization of 2,3-cyclic nucleotide 3-phosphodiesterase in human erythrocyte membranes
Biochim. Biophys. Acta
649
587-594
1981
Homo sapiens
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
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
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
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
Anal. Biochem.
202
6-9
1992
Homo sapiens
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
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
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
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
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)
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
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
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
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
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
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
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