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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
3.1.4.37
-
RECOMMENDED NAME
GeneOntology No.
2',3'-cyclic-nucleotide 3'-phosphodiesterase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
show the reaction diagram
-
-
-
-
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate
show the reaction diagram
general acid/general base catalysis by H310, H231 and a water molecule, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-, P06961
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2',3'-cyclic AMP phosphodiesterase
-
-
-
-
2',3'-cyclic nucleoside monophosphate phosphodiesterase
-
-
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
P09543
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
-
2',3'-cyclic nucleotide 3'-phosphohydrolase
-
-
-
-
2',3'-cyclic nucleotide phosphohydrolase
-
-
-
-
2',3'-cyclic nucleotide-3'-phosphohydrolase
-
-
2',3'-cyclic phosphodiesterase
-
-
2',3'-cyclic-nucleotide 3'-phosphodiesterase type I
P09543
-
2':3'-CNMP-3'-ase
-
-
2':3'-cyclic nucleotide 3'-phosphodiesterase
-
-
-
-
CNP
-
-
-
-
CNP
P09543
-
CNP1
-
isoform
CNPase
-
-
-
-
CNPase
-
-
CNPase
-
-
CNPase I
P09543
-
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'-
-
-
-
-
PNKP
Clostridium thermocellum
-
-
CAS REGISTRY NUMBER
COMMENTARY
60098-35-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. amyloliquefacus
-
-
Manually annotated by BRENDA team
overview, calf
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
Clostridium thermocellum
polynucleotide kinase-phosphatase
-
-
Manually annotated by BRENDA team
zebrafish
-
-
Manually annotated by BRENDA team
2',3'-cyclic phosphodiesterase activity of the C-terminal HD domain of the multifunctional enzyme tRNA nucleotidyltransferase, EC 2.7.7.25
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
2 isoforms: CNP1 and CNP2
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
no activity in Rattus norvegicus
in olfactory ensheathing cells
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
bullfrog
-
-
Manually annotated by BRENDA team
2 isoenzymes of 46 and 48 kDa
-
-
Manually annotated by BRENDA team
2 isoforms: CNP1 and CNP2 differing by a 20-amino acid extension at the N-terminus
-
-
Manually annotated by BRENDA team
2 isoforms: CNP1 and CNP2, encoded by a single gene
-
-
Manually annotated by BRENDA team
isoform CNP2 fused to GFP
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, 1-2 days old, 2 isoforms: CNP1 and CNP2 differing by a 20-amino acid extension exclusive to CNP2
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, adult, 2 isoforms: CNP1 and CNP2, produced by ribosome initiation at different AUG codons
-
-
Manually annotated by BRENDA team
three-week-old male Crl:CD (SD) IGS rats
-
-
Manually annotated by BRENDA team
Wistar and Lister strains, age ranging from postnatal day 3 to 60
-
-
Manually annotated by BRENDA team
Wistar rats, 2 months old
-
-
Manually annotated by BRENDA team
Wistar rats, from post-natal days 5 to 90, hypothyroid and controls
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-etheno-2-azaadenosine-2',3'-cyclic monophosphate + H2O
etheno-2-azaadenosine-2'-monophosphate
show the reaction diagram
-
-
-
-
?
1,N6-ethenoadenosine-2',3'-cyclic monophosphate + H2O
ethenoadenosine-2'-monophosphate
show the reaction diagram
-
-
-
-
?
2', 3'-cyclic ribonucleotide
ribonucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
-
-
?
2',3'-cAMP + H2O
2'-AMP
show the reaction diagram
-
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'-cAMP + H2O
2'-AMP + 3'-AMP
show the reaction diagram
-, P06961
-
-
-
-
2',3'-cAMP + H2O
3'-AMP + ?
show the reaction diagram
-
the exclusive formation of 3'-AMP is due to the P-O2' bond having lower activation energy and is not the result of steric exclusion at enzyme active site, kinetic evidence that hydrolysis of 2',3'-cAMP into 3'-AMP is nonspecific. Modeling of 2',3'-cyclic nucleotide into the active site of a EAL domain PDE, overview
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
2'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP
show the reaction diagram
-
-
-
-
?
2',3'-cGMP + H2O
2'-GMP + 3'-GMP
show the reaction diagram
-, P06961
-
-
-
-
2',3'-cNADP+ + H2O
2'-NADP+
show the reaction diagram
-
-
-
-
?
2',3'-cNADP+ + H2O
2'-NADP+
show the reaction diagram
-
-
-
?
2',3'-cNADP+ + H2O
2'-NADP+
show the reaction diagram
-
-
-
-
?
2',3'-cNADP+ + H2O
NADP+
show the reaction diagram
-
-
-
?
2',3'-cUMP + H2O
2'-UMP
show the reaction diagram
-
-
-
-
?
2',3'-cUMP + H2O
2'-UMP
show the reaction diagram
-
-
-
-
?
2',3'-cUMP + H2O
2'-UMP
show the reaction diagram
-
-
-
-
?
2',3'-cUMP + H2O
2'-UMP
show the reaction diagram
-
-
-
-
?
2',3'-cyclic NADP+ + H2O
NADP+
show the reaction diagram
-
-
-
-
-
2',3'-cyclic NADP+ + H2O
NADP+
show the reaction diagram
-
-
-
?
2',3'-cyclic NADP+ + H2O
NADP+
show the reaction diagram
-
-
-
-
-
2',3'-cyclic-2-aza-e-AMP + H2O
2'-2-aza-e-AMP
show the reaction diagram
-
-
-
-
?
2',3'-cyclic-e-AMP + H2O
2'-e-AMP
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-, P06961
-
-
-
-
3'-AMP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-, P06961
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
-, P06961
-
-
-
-
bis(p-nitrophenyl)phosphate + H2O
?
show the reaction diagram
-
non-specific substrate
-
-
?
bis-p nitrophenyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
-, P06961
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-, P06961
-
-
-
-
CTP + H2O
CDP + phosphate
show the reaction diagram
-, P06961
-
-
-
-
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
Clostridium thermocellum
-
-
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
P09543
-
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
-
-
-
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
-, P06961
best substrate
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
-, P06961
natural substrate, the 2',3'-cyclic phosphodiesterase activity of the C-terminal HD domain of tRNA nucleotidyltransferase, EC 2.7.7.25, is involved in the repair of the 3-CCA end of tRNA
-
?
cyclic 2',3'-CMP + H2O
2'-CMP
show the reaction diagram
-, P06961
low activity
-
?
cyclic 2',3'-GMP + H2O
2'-GMP
show the reaction diagram
-, P06961
high activity
-
?
NADP+ + H2O
NAD+ + phosphate
show the reaction diagram
-, P06961
-
-
-
-
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-, P06961
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
-
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
activity resides in the C-terminus
-
?
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
plays a role in cytoskeletal rearrangement, cell morphology and cell process outgrowth, increased expression of CNP is a marker for oligodendrocyte development
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-, P06961
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-, P06961
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
not: 2',3'-cyclic esters in cyclic phosphate-terminated oligoribonucleotides or in nucleoside 5'-phosphate, 2',3'-cyclic phosphate
-
-
-
additional information
?
-
-
three enzyme forms
-
-
-
additional information
?
-
-
not: 3',5'-cyclic nucleotides
-
-
-
additional information
?
-
-
not: 3',5'-cyclic nucleotides
-
-
-
additional information
?
-
-
not: 3',5'-cyclic nucleotides
-
-
-
additional information
?
-
-, P06961
not: nucleoside 3',5'-cyclic phosphate
-
?
additional information
?
-
-
early stages of myelin formation
-
-
-
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 and nuclear factor-1 in the regulation of CNP1 expression
-
?
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 is involved in mediating process formation in oligodendrocytes
-
-
-
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
?
-
-
endogenous Nogo-A interacts with the endogenous CNP in vitro and in vivo
-
-
-
additional information
?
-
-
substrate specificities and activities of RocR, DGC2, YybT, YtqI, 3DMA, and PaAcpH with 2',3'-cAMP, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside 2',3'-cyclic phosphate + H2O
nucleoside 2'-phosphate
show the reaction diagram
-
plays a role in cytoskeletal rearrangement, cell morphology and cell process outgrowth, increased expression of CNP is a marker for oligodendrocyte development
-
?
cyclic 2',3'-AMP + H2O
2'-AMP
show the reaction diagram
-, P06961
natural substrate, the 2',3'-cyclic phosphodiesterase activity of the C-terminal HD domain of tRNA nucleotidyltransferase, EC 2.7.7.25, is involved in the repair of the 3-CCA end of tRNA
-
?
additional information
?
-
-
early stages of myelin formation
-
-
-
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 and nuclear factor-1 in the regulation of CNP1 expression
-
?
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 is involved in mediating process formation in oligodendrocytes
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
slight stimulation
Co2+
-
activation of activity against bis-p-nitrophenyl phosphate
Mg2+
-
slight stimulation
Mg2+
-, P06961
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
Mg2+
-
assay buffer
Mg2+
-
activates
Mn2+
-
slight stimulation
Mn2+
-
slight stimulation
Mn2+
-
slight stimulation
Mn2+
Clostridium thermocellum
-
required
Ni2+
-, P06961
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+
Mn2+
-
activates
additional information
-
-
additional information
-
-
additional information
-
no divalent metals required
additional information
-
-
additional information
-
no divalent metals required
additional information
-, P06961
metal-independent 2',3'-cyclic phosphodiesterase activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-AMP
-
product inhibitor
5'-AMP
-, P06961
-
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
arsenate
-
-
arsenite
-
-
Atractyloside
-
noncompetitive
basic fibroblast growth factor
-
-
-
Ca2+
-
74% inhibition at 0.5 mM
Co2+
-, P06961
-
Cu2+
-
95% inhibition at 0.5 mM
Cu2+
-
75% inhibition at 2 mM
Cu2+
-
93% inhibition at 0.5 mM
Cu2+
-, P06961
-
Diethylpyrocarbonate
-
pH 6.5, 22C, time-dependent inhibition, kinetics, completely reversed by 0.5 M hydroxylamine
diisopropyl fluoroacetate
-
-
Elastase
-
little inactivation
-
Fe2+
-
33% inhibition at 0.5 mM
Fe3+
-
66% inhibition at 0.5 mM
Guanidinium chloride
-
-
iodoacetamide
-
-
KCN
-
62% inhibition of the catalytic fragment of CNP1
lead
-
90 days exposure of young adult rats to lead in drinking water, decrease both in enzyme protein content and activity
methyl methanethiosulfonate
-
42% inhibition of the catalytic fragment of CNP1
NaCl
-
31% inhibition at 0.4 mM
p-chloromercuribenzoate
-
98% inhibition at 0.2 mM
physostygmine
-
-
Polynucleotides
-
polyA, polyU
Sulfhydryl reagent
-
-
-
theophylline
-
-
tRNA
-, P06961
10 nM, strong competitive inhibition of 2',3'-cyclic phosphodiesterase activity, inhibition is abolished by addition of Mg2+, Mn2+ or Ca2+, but not of Ni2+
Trypsin
-
inactivation
-
Trypsin
-
-
-
Trypsin
-
-
-
tubercidin
-
-
Zn2+
-
82% inhibition at 0.5 mM
Zn2+
-
14% inhibition at 2 mM
Zn2+
-
87% inhibition at 0.5 mM
Zn2+
-, P06961
-
additional information
-
-
-
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
-
not inhibited by dithiothreitol
-
additional information
-, P06961
not inhibited by Mg2+, Mn2+, Ca2+ or Ni2+
-
additional information
-
actinomycin D or cycloheximide completely inhibits the dibutyryl-cAMP-induced accumulation of CNP1 mRNA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bovine serum albumin
-
-
-
Bovine serum albumin
-
-
-
cytosine arabinoside
-
-
Hexadecyltrimethylammonium bromide
-
-
histone F3
-
reverses inhibition by polynucleotides
-
lipopolysaccharide
-
enzyme expression is significantly up-regulated in microglial activation induced in vitro by lipopolysaccharide
myelin basic protein
-
reverses inhibition by polynucleotides
-
Na-deoxycholate
-
haemolysed precipitate
Na-deoxycholate
-
-
Na-deoxycholate
-
-
protein activator
-
-
-
Triton X-100
-
-
Triton X-100
-
-
Triton X-100
-
-
Triton X-100
-
-
Lubrol WX
-
-
-
additional information
-
solublization of the enzyme by elastase or trypsin
-
additional information
-
-
-
additional information
-
-
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
1,N6-Etheno-2-azaadenosine-2',3'-cyclic monophosphate
-
-
8.3
-
1,N6-Ethenoadenosine-2',3'-cyclic monophosphate
-
rat brain
0.25
-
2',3'-cAMP
-
-
0.32
-
2',3'-cAMP
-
H7-zRICH-WT mutant
0.37
-
2',3'-cAMP
-
-
0.38
-
2',3'-cAMP
-
pig cerebral white matter
0.39
-
2',3'-cAMP
-
H7-zRICH-C339A mutant
0.49
-
2',3'-cAMP
-, P06961
+/- 0.04
0.537
-
2',3'-cAMP
-
full-length protein
1.64
-
2',3'-cAMP
-
pH 6.2, 37C
1.9
-
2',3'-cAMP
-
bovine brain
2.15
-
2',3'-cAMP
-
pH 6.2, 37, treatment with lead
2.5
-
2',3'-cAMP
-
H7-zRICH-R332A mutant
6
-
2',3'-cAMP
-
rat brain
13.1
-
2',3'-cAMP
-
-
0.8
-
2',3'-cCMP
-
bovine brain
5.6
-
2',3'-cCMP
-
bovine brain, elastase fragment
25.2
-
2',3'-cCMP
-
-
0.57
-
2',3'-cGMP
-
bovine brain
1.6
-
2',3'-cGMP
-, P06961
+/- 0.22
9.2
-
2',3'-cGMP
-
-
0.098
-
2',3'-cNADP
-
pH 6, 25C, H309L mutant CNP1
0.1
-
2',3'-cNADP
-
pH 6, 25C, H309F mutant CNP1
0.104
-
2',3'-cNADP
-
pH 6, 25C, H230L mutant CNP1
0.119
-
2',3'-cNADP
-
pH 6, 25C, H230F mutant CNP1
0.23
-
2',3'-cNADP
-
bovine spinal cord
0.231
-
2',3'-cNADP
-
pH 6, 25C, C231A mutant CNP1
0.237
-
2',3'-cNADP
-
pH 6, 25C, recombinant full-length CNP1
0.241
-
2',3'-cNADP
-
pH 6, 25C, C314S mutant CNP1
0.295
-
2',3'-cNADP
-
pH 6, 25C, catalytic fragment of CNP1 corresponding to the C-terminal 250 amino acids
0.333
-
2',3'-cNADP
-
pH 6, 25C, C314A mutant CNP1
0.354
-
2',3'-cNADP
-
pH 6, 25C, C236A mutant CNP1
0.379
-
2',3'-cNADP
-
pH 6, 25C, C236S mutant CNP1
0.47
-
2',3'-cNADP
-
rat brain
0.473
-
2',3'-cNADP
-
pH 6, 25C, C231S mutant CNP1
0.51
-
2',3'-cNADP
-
rat liver
0.55
-
2',3'-cNADP
-
-
8.3
-
2',3'-cUMP
-
bovine brain
25.3
-
2',3'-cUMP
-
-
0.76
-
2'-AMP
-, P06961
+/- 0.13
0.046
-
3'-AMP
-
-
0.19
-
ADP
-, P06961
+/- 0.02
0.18
-
ATP
-, P06961
+/- 0.01
0.16
-
bis-p-nitrophenyl phosphate
-
-
0.53
-
CDP
-, P06961
+/- 0.09
0.13
-
CTP
-, P06961
+/- 0.01
0.49
-
cyclic 2',3'-AMP
-, P06961
pH 7, 37C
3.9
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H376D, pH 7.5, 45C
4.7
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H376N, pH 7.5, 45C
6.6
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236N, pH 7.5, 45C
7.8
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236A, pH 7.5, 45C
18
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236E, pH 7.5, 45C; mutant D392E, pH 7.5, 45C; wild-type, pH 7.5, 45C
20
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189D, pH 7.5, 45C
24
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H323Q, pH 7.5, 45C
28
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189E, pH 7.5, 45C
29
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189A, pH 7.5, 45C
31
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D392N, pH 7.5, 45C
32
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H323A, pH 7.5, 45C
60
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant R237Q, pH 7.5, 45C
62
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D233E, pH 7.5, 45C
77
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant R237A, pH 7.5, 45C
100
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D392A, pH 7.5, 45C; mutant R237K, pH 7.5, 45C
1.6
-
cyclic 2',3'-GMP
-, P06961
pH 7, 37C
0.15
-
NADP
-, P06961
+/- 0.02
6.2
-
p-nitrophenyl phosphate
-, P06961
+/- 0.46
0.1
-
diphosphate
-, P06961
+/- 0.004
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
in the prescence of serum albumin or hexadecyltrimethylammonium bromide
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
three enzyme forms
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.63
-
2',3'-cAMP
-, P06961
+/- 0.48
118
-
2',3'-cAMP
-
full-length protein
1.97
-
2',3'-cGMP
-, P06961
+/- 0.08
1.15
-
2',3'-cNADP
-
pH 6, 25C, H230F mutant CNP1
1.16
-
2',3'-cNADP
-
pH 6, 25C, H230L mutant CNP1
1.27
-
2',3'-cNADP
-
pH 6, 25C, H309L mutant CNP1
1.35
-
2',3'-cNADP
-
pH 6, 25C, H309F mutant CNP1
6.08
-
2',3'-cNADP
-
pH 6, 25C, H230L mutant CNP1; pH 6, 25C, H309L mutant CNP1
594
-
2',3'-cNADP
-
pH 6, 25C, C314S mutant CNP1
825
-
2',3'-cNADP
-
pH 6, 25C, C231S mutant CNP1
968
-
2',3'-cNADP
-
pH 6, 25C, C231A mutant CNP1
1107
-
2',3'-cNADP
-
pH 6, 25C, C236S mutant CNP1
1110
-
2',3'-cNADP
-
pH 6, 25C, C236S mutant CNP1
1116
-
2',3'-cNADP
-
pH 6, 25C, C314A mutant CNP1
1120
-
2',3'-cNADP
-
pH 6, 25C, C314A mutant CNP1
1130
-
2',3'-cNADP
-
pH 6, 25C, C397S mutant CNP1
1132
-
2',3'-cNADP
-
pH 6, 25C, C397S mutant CNP1
1195
-
2',3'-cNADP
-
pH 6, 25C, recombinant full-length wild-type CNP1
1200
-
2',3'-cNADP
-
pH 6, 25C, recombinant full-length wild-type CNP1
1476
-
2',3'-cNADP
-
pH 6, 25C, C236A mutant CNP1
1480
-
2',3'-cNADP
-
pH 6, 25C, C236A mutant CNP1
1690
-
2',3'-cNADP
-
pH 6, 25C, catalytic fragment of CNP1 corresponding to the C-terminal 250 amino acids
3.09
-
2'-AMP
-, P06961
+/- 0.14
1.24
-
ADP
-, P06961
+/- 0.07
3.78
-
ATP
-, P06961
+/- 0.12
4.83
-
CDP
-, P06961
+/- 0.39
3.36
-
CTP
-, P06961
+/- 0.17
0.031
0.51
cyclic 2',3'-AMP
-, P06961
pH 7, 37C
1.45
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189A, pH 7.5, 45C
1.8
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D392A, pH 7.5, 45C
3.2
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H376D, pH 7.5, 45C
3.25
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D233E, pH 7.5, 45C
4.5
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236A, pH 7.5, 45C
5.1
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H376N, pH 7.5, 45C
5.8
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236N, pH 7.5, 45C
6
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D236E, pH 7.5, 45C
6.5
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H323Q, pH 7.5, 45C
7.63
-
cyclic 2',3'-AMP
-, P06961
pH 7, 37C
8.6
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant R237A, pH 7.5, 45C
8.9
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
wild-type, pH 7.5, 45C
9.1
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H323A, pH 7.5, 45C
15.9
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D392E, pH 7.5, 45C
17.2
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189E, pH 7.5, 45C
18.7
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant D392N, pH 7.5, 45C
20.2
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant R237Q, pH 7.5, 45C
26.2
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant R237K, pH 7.5, 45C
34.3
-
cyclic 2',3'-AMP
Clostridium thermocellum
-
mutant H189D, pH 7.5, 45C
1.97
-
cyclic 2',3'-GMP
-, P06961
pH 7, 37C
2.94
-
cyclic 2',3'-GMP
-, P06961
pH 7, 37C
14.9
-
NADP
-, P06961
+/- 0.5
10.3
-
p-nitrophenyl phosphate
-, P06961
+/- 0.28
2.51
-
diphosphate
-, P06961
+/- 0.05
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
220
-
2',3'-cAMP
-
full-length protein
942
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.5
-
2'-AMP
-
-
0.59
-
5'-AMP
-, P06961
-
0.00000168
-
tRNA
-, P06961
hydrolysis of cyclic 2',3'-AMP
0.29
-
tRNA
-, P06961
with ATP
1.08
-
tRNA
-, P06961
with 2'-AMP
1.68
-
tRNA
-, P06961
with 2',3'-cAMP
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.066
-
-
rabbit, adrenal gland
0.133
-
-
2',3'-cAMP, hole mitochondria
0.24
-
-
mitochondrial inner membrane
0.28
-
-
mitochondrial outer membrane
1.49
-
-, P06961
+/- 0.08, ADP
2.36
-
-, P06961
+/- 0.10, 2',3'-cGMP
3.01
-
-, P06961
+/- 0.06, diphosphate
3.21
-
-, P06961
+/- 0.1, 2',3'-cAMP
3.71
-
-, P06961
+/- 0.17, 2'-CMP
4.03
-
-, P06961
+/- 0.20, CTP
4.53
-
-, P06961
+/- 0.14, ATP
5.8
-
-, P06961
+/- 0.47, CDP
6.28
-
-
2',3 '-cCMP, fish retina
11.2
-
-
pH 6.2, 37, treatment with lead
12.4
-
-, P06961
+/- 0.34, p-nitrophenyl phosphate
13.4
-
-
pH 6.2, 37C
17.9
-
-, P06961
+/- 0.6, NADP
35
-
-
2',3'-cAMP, frog brain
130.6
-
-
ZRICH-WT-enzyme
280
-
-
2',3'-cGMP
600
-
-
2',3'-cUMP
2090
-
-
2',3'-cAMP
2140
-
-
2',3'-cCMP
2300
-
-
-
2680
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
mitochondrial inner and outer membrane, effect of chronic ethanol ingestion
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
activity against bis-p-nitrophenyl phosphate
5.4
6.2
-
without detergent
6
7
-
-
6
-
-
in the prescence of serum albumin or hexadecyltrimethylammonium bromide
6
-
-
assay at
6.2
-
-
-
6.6
-
-
-
7
-
-
-
7
-
-, P06961
-
8
8.3
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
6.5
-
-
4
8.5
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
-
37
-
-, P06961
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
37
-
30C: optimum, 37C: 90% of optimum activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
9.3
-
isoelectric focusing
9
-
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
9.2
-
-
theoretical value
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
two enzyme isoforms in chicken, just one isoform in bullfrog
Manually annotated by BRENDA team
-
white matter
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
subventricular zone rostral extension, CNPase expression pattern during development from postnatal day 3 to 60
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
CNP is associated with tubulin from brain
Manually annotated by BRENDA team
-
embryonic brain
Manually annotated by BRENDA team
-
developing brain
Manually annotated by BRENDA team
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
Manually annotated by BRENDA team
-
cerebellar, both isoforms CNP1 and CNP2
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
with age, CNP accumulates throughout brain white matter accompanied by proteolytic fragments of CNP. Equal increase in both isoforms CNP1 and CNP2
Manually annotated by BRENDA team
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
Manually annotated by BRENDA team
-
ubiquitinated CNP
Manually annotated by BRENDA team
-
ATCC CRL 8305, thyroid cells, CNP is firmly associated with FRTL-5 cells
Manually annotated by BRENDA team
-
olfactory bulb ensheathing glia in explant cultures
Manually annotated by BRENDA team
-
neonatal mouse brain cells
Manually annotated by BRENDA team
-
from newborn rat brain
Manually annotated by BRENDA team
-
oligodendrocyte-enriched cultures of neonatal rat brain glial cells, CNP2
Manually annotated by BRENDA team
-
abundantly in the cytoplasmic compartments of CNS myelin
Manually annotated by BRENDA team
-
myelinating cell
Manually annotated by BRENDA team
-
with age, CNP accumulates in myelin accompanied by proteolytic fragments of CNP. Equal increase in both isoforms CNP1 and CNP2
Manually annotated by BRENDA team
-
peripheral nerve sheath tumors, immunohistochemic and histochemic analysis of 63 tumors from 44 cattle: 35 schwannomas, 9 neurofibromas, 14 hybrid (neurofibroma-schwannoma) tumors, and 5 malignant peripheral nerve sheath tumors
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
olfactory bulb ensheathing glia in explant cultures
Manually annotated by BRENDA team
-
olfactory ensheathing cells, the nonmyelinating glial cells of the olfactory nerves and bulb, in situ immunohistochemic analysis, overview
Manually annotated by BRENDA team
-
bipotential proliferating and differentiating CG-4 cells
Manually annotated by BRENDA team
-
the two isoforms CNP1 and CNP2 are differentially regulated during the process of maturation, CNP expression pattern
Manually annotated by BRENDA team
-
cerebellar, both isoforms CNP1 and CNP2
Manually annotated by BRENDA team
-
peripheral nerve sheath tumors, immunohistochemic and histochemic analysis of 63 tumors from 44 cattle: 35 schwannomas, 9 neurofibromas, 14 hybrid (neurofibroma-schwannoma) tumors, and 5 malignant peripheral nerve sheath tumors
Manually annotated by BRENDA team
-
optic nerve regenerating retinas
Manually annotated by BRENDA team
-
presence of enzyme immunoreactive material at birth, progressive reduction with age with complete loss at postnatal day 18
Manually annotated by BRENDA team
-
myelin sheaths of the cerebral white matter
Manually annotated by BRENDA team
additional information
-
CNP2 is barely detectable in testis and thymus
Manually annotated by BRENDA team
additional information
-
MO3.13 cell, ubiquitinated CNP
Manually annotated by BRENDA team
additional information
-
spatiotemporal distribution of CNPase, an early oligodendrocyte/Schwann cell marker, overview
Manually annotated by BRENDA team
additional information
-
bovine peripheral nerve sheath tumors commonly have both schwannomatous and neurofibromatous areas
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
abundantly in the cytoplasmic compartments of CNS myelin
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
single and double-unit membrane, from non-compact regions of myelin
Manually annotated by BRENDA team
-
exclusively associated with the cytosolic side of the membrane; myelin membranes
Manually annotated by BRENDA team
-
cytosolic side of the membrane
Manually annotated by BRENDA team
-
myelin membranes
Manually annotated by BRENDA team
-
cytosolic side of the membrane
Manually annotated by BRENDA team
-
integral membrane protein, inner and outer mitochondrial membrane
Manually annotated by BRENDA team
-
myelin membranes
Manually annotated by BRENDA team
-
membrane-bound, microtubule-associated protein, membrane anchor for tubulin
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
tubulin from brain, microtubule-associated protein, membrane anchor for tubulin, membrane-bound
Manually annotated by BRENDA team
-
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.
Manually annotated by BRENDA team
-
of marrow stromal cell
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution of CNP
-
Manually annotated by BRENDA team
additional information
-
partially localize within lipid rafts
-
Manually annotated by BRENDA team
additional information
-
ubiquitinated CNP in the Triton X-100 insoluble lipid raft associated fractions of myelin
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10000
-
-
sedimentation analysis in presence of bovine serum albumin, bovine brain
23000
-
-
gel filtration
31000
-
-
gel filtration
31000
-
-
gel filtration
36500
-
-
sedimentation coefficient
40000
-
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
41200
43900
-
MALDI TOF mass spectrometry
44850
-
-
sequence analysis, bovine brain
45100
-
-
sequence analysis, human brain
46000
-
-
endogenous CNP, immunoblot analysis
47000
-
-
endogenous CNP, SDS-PAGE
47580
-
-
theoretical value
48000
-
-
endogenous CNP, immunoblot analysis
49000
51000
-
antibody column
50000
-
-
sucrose density gradient centrifugation without bovine serum albumin
50000
-
-
GC-CNP transfected MO3.13 cells, immunoblot analysis
50000
-
-
2D electrophoresis and immunoblotting, lipid raft fraction from a young monkey
55000
-
-
gel filtration
60000
-
-
GC-CNP transfected MO3.13 cells, immunoblot analysis
100000
-
-
gel filtration and gel electrophoresis under non reducing conditions, sucrose density gradient centrifugation
100000
-
-
sucrose density gradient centrifugation in the presence of bovine serum albumin or human gamma globulin or carbonic anhydrase or myelin basic protein
120000
-
-
gel filtration, native conditions, bovine brain
128000
-
-
gel electrophoresis, second major band, microsomes
150000
-
-
GC-CNP/YN-Ub complex transfected MO3.13 cells, immunoblot analysis
250000
-
-
GC-CNP/YN-Ub complex transfected MO3.13 cells, immunoblot analysis
263000
-
-
gel electrophoresis, first major band, microsomes
additional information
-
-
in lipid raft fraction from an aged monkey, evidence of sequential CNP proteolysis, abundance of CNP immunoreactive higher molecular weight material
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 33000, SDS-PAGE
?
-
x * 44000-47000, SDS-PAGE
?
-
x * 110000 SDS-PAGE
?
-
x * 51000, SDS-PAGE
?
-
x * 24000, SDS-PAGE
?
-
27000-31000, SDS-PAGE
?
-
x * 74000, SDS-PAGE
?
-
x * 46000, major CNP isoenzyme, x * 48000, minor CNP isoenzyme
?
-
x * 46000, CNP1, x * 48000, CNP2
?
-
x * 46000, CNP1, x * 48000, CNP2, SDS-PAGE
?
-
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
-
1* 44000 + 1* 54000, SDS-PAGE
dimer
-
1* 54000 + 1* 51000, SDS-PAGE
dimer
-
1 * 44600 + 1* 45900, SDS-PAGE
dimer
-, P06961
-
monomer
-
1 * 30000, SDS-PAGE
oligomer
-
50000-100000, SDS-PAGE
oligomer
-, P06961
-
monomer
-, P06961
predominantly
additional information
-
enzyme interacts with tubulin, binding preferentially to tubulin heterodimers and inducing assembly of mircotubulues by cooperation with tubulin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
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
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
-
isoprenylated at Cys-397
side-chain modification
-
CNP is isoprenylated and palmitoylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catalytic fragment of enzyme
-
modeling of enzyme N-terminal region and simulation of docking of nucleotides
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
50% loss of activity after 5 min
50
70
-
inactivation
50
-
-
completely inactivated after 5 min
55
-
-
no loss of activity after 10 min
60
-
-
85% loss of activity after 15 min
65
75
-
increase in the melting temperature induced by both pH 5.5 and high salt concentration. At pH 5.5, without NaCl: ca. 68C and with 500 mM NaCl: ca. 75C. At pH 7.5 without NaCl and with 500 mM NaCl: ca. 70C
65
-
-
20% loss of activity after 10 min
80
-
-
82.2% loss of activity after 10 min
100
-
-
80% loss of activity, and completely eliminated after 20 min, Co2+ protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing, not affected by several cycles
-
dilution, inactivates
-
freezing and thawing, inactivates
-
serum albumin, 2'-AMP and NaCl, stabilizes
-
stable
-, P06961
25 mM citric acid, 50 mM Na2HPO4 buffer, pH 6.2
-
bovine serum albumin, stable for 6 months
-
freezing and thawing, not affected by several cycles
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
at a final concentration up to 4% v/v of the total volume, no effect on CNP1 activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-30C, stable for several months
-
4C, stable for 2 days
-
0-4C, 5 mM Tris-HCl buffer, pH 7.6, stable for 2 months
-
4C, 6 months, more than 90% of activity retained
-
4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
-, P06961
4C, for weeks
-
-20C for at least 1 month or at 4C for 3 weeks
-
-80C for 24 h, 90% loss of activity
-
-70C, stable for at least 5 months
-
4C, Tris-acetate buffer, 0.5 mM dithiothreitol, pH 7.6, 10% glycerol, protease inhibitor mix, 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1990fold
-
partial, by delipidation, solubilization, gel chromatography, resolubilization, ion-exchange chromatography and affinity chromatography
-
recombinant tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
-, P06961
by Ni-affinity chromatography followed by gel filtration
-
immunopurification, to homogeneity
-
recombinant CNP1 and C-terminal deletion mutant
-
recombinant wild-type and mutant CNP1
-
partial, 1196.4fold band 1, 739.9fold band 2, microsomes
-
10000fold
-
16000fold to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
bovine brain
-
GC-CNP encoding 155238 aa of GFP fused to the N-terminus of CNP co-transfected with YN-Ub into COS-7 cells
-
; tRNA nucleotidyltransferase, EC 2.7.7.25, with its HD domain possessing 2',3'-cyclic phosphodiesterase activity
-, P06961
expressed in HEK-293 cells
-
GC-CNP encoding 155238 aa of GFP fused to the N-terminus of CNP co-transfected with YN-Ub into MO3.13 cells
-
human brain, subcloned into a plasmid vector
-
overexpression in transgenic mice
-
CNP gene with various deletions of the CNP promoter, expression in rat C6 cells, regulation of CNP1 promoter activity by cAMP
-
subcloned into pTH27, expressed in Escherichia coli Rosetta (DE3) with a TEV protease-cleavable His-tag
-
expression in Saccharomyces cerevisiae
-
expression with His-tag
-
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
-
subcloning into the Bluescript vector
-
wild type and mutant CNP proteins are produced in vitro in rabbit reticulocyte lysate in the presence of S-methionine
-
wild-type and mutant CNP1, expression in Escherichia coli BL21
-
wild-type and mutant CNP2, expression in 293T human kidney fibroblast cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
treatment of purified adult canine olfactory ensheathing cells with fibroblast growth factor-2 significantly reduces CNPase expression at the protein and mRNA level
-
expression of CNP is reduced by 10% in schizophrenics compared with controls, but the difference is not significant
-
CNP mRNA levels do not change with age
-
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D233A
Clostridium thermocellum
-
catalytic activity is neligible
D233E
Clostridium thermocellum
-
decrease in catalytic efficiency by factor 9
D233N
Clostridium thermocellum
-
catalytic activity is neligible
D236A
Clostridium thermocellum
-
increase in enzyme affinity for substrate
D236E
Clostridium thermocellum
-
kinetics similar to wild-type
D236N
Clostridium thermocellum
-
increase in enzyme affinity for substrate
D392A
Clostridium thermocellum
-
decrease of both kcat and Km value
D392E
Clostridium thermocellum
-
2fold increase in kcat value without affecting Km value
D392N
Clostridium thermocellum
-
2fold increase in kcat value without affecting Km value
H189A
Clostridium thermocellum
-
slight increase of Km value with 6fold decrease in kcat value
H189D
Clostridium thermocellum
-
4fold increase in kcat value without affecting Km value
H189E
Clostridium thermocellum
-
2fold increase in kcat value without affecting Km value
H323A
Clostridium thermocellum
-
kinetics similar to wild-type
H323Q
Clostridium thermocellum
-
kinetics similar to wild-type
H376D
Clostridium thermocellum
-
60% increase in catalytic efficiency
H376N
Clostridium thermocellum
-
twofold increase in catalytic efficiency
R237A
Clostridium thermocellum
-
4fold increase in Km value
R237K
Clostridium thermocellum
-
6fold increase in Km value
D21A
-, P06961
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D23A
-, P06961
tRNA nucleotidyltransferase mutant, EC 2.7.7.25, no effect on the 2',3'-cyclic phosphodiesterase activity
D256A
-, P06961
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
D306A
-, P06961
HD domain mutant with 2',3'-cyclic phosphodiesterase activity
H225A
-, P06961
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
C231A
-
CNP1 catalytic fragment mutant, kinetics
C231S
-
CNP1 catalytic fragment mutant, kinetics
C236A
-
CNP1 catalytic fragment mutant, kinetics
C236S
-
CNP1 catalytic fragment mutant, kinetics
C314A
-
CNP1 catalytic fragment mutant, kinetics
C314S
-
CNP1 catalytic fragment mutant, kinetics
C397S
-
CNP1 catalytic fragment mutant, kinetics
H230A/T232A/H309A/T311A
-
catalytically inactive
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
S22A
-
CNP2 mutant with reduced phosphate incorporation
S23A
-
CNP2 mutant
S9A
-
CNP2 mutant with reduced phosphate incorporation
S9A/S22A
-
CNP2 double mutant without phosphate incorporation
R237Q
Clostridium thermocellum
-
3fold increase in Km value
additional information
-
-
H305A
-, P06961
HD domain mutant without detectable 2',3'-cyclic phosphodiesterase activity
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
M21L
-
CNP2 mutant
additional information
-
CNP1: N-terminal deletion mutants, catalytic fragment corresponding to the last C-terminal 250 amino acids
additional information
-
C-terminal deletion of 13 amino acids of CNP1 leads to an abnormal microtubule distribution in the cell
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
no association between genetic variation in the CNP enzyme gene and schizophrenia in the Han Chinese population
medicine
-
CNPase is associated with multiple sclerosis
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
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