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Literature summary for 3.1.4.37 extracted from

  • Raasakka, A.; Kursula, P.
    The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and function (2014), Neurosci. Bull., 30, 956-966.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure analysis Mus musculus
structure analysis Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information generation of inactive mutants truncated after amino acid 164 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol isoform I Homo sapiens 5829
-
membrane membrane-anchored enzyme present on the cytosolic side of non-compact myelin Oryctolagus cuniculus 16020
-
mitochondrion isoform II, intermembrane space Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2',3'-cyclic AMP + H2O Mus musculus
-
2'-AMP
-
?
2',3'-cyclic AMP + H2O Homo sapiens
-
2'-AMP
-
?
2',3'-cyclic AMP + H2O Rattus norvegicus
-
2'-AMP
-
?
2',3'-cyclic AMP + H2O Oryctolagus cuniculus
-
2'-AMP
-
?
nucleoside 2',3'-cyclic phosphate + H2O Mus musculus
-
nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O Homo sapiens
-
nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O Rattus norvegicus
-
nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O Oryctolagus cuniculus
-
nucleoside 2'-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
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
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain
-
Homo sapiens
-
brain
-
Rattus norvegicus
-
brain
-
Oryctolagus cuniculus
-
myelin membrane the enzyme is most abundant protein in non-compact myelin and the third-most abundant protein overall in CNS myellin Homo sapiens
-
myelin membrane the enzyme is one of the most abundant proteins in CNS myelin Mus musculus
-
myelin membrane the enzyme is one of the most abundant proteins in CNS myelin Rattus norvegicus
-
myelin membrane the enzyme is one of the most abundant proteins in CNS myelin Oryctolagus cuniculus
-
olfactory ensheathing cell
-
Homo sapiens
-
peripheral nervous system
-
Mus musculus
-
peripheral nervous system
-
Homo sapiens
-
peripheral nervous system
-
Rattus norvegicus
-
peripheral nervous system
-
Oryctolagus cuniculus
-
Schwann cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cyclic AMP + H2O
-
Mus musculus 2'-AMP
-
?
2',3'-cyclic AMP + H2O
-
Homo sapiens 2'-AMP
-
?
2',3'-cyclic AMP + H2O
-
Rattus norvegicus 2'-AMP
-
?
2',3'-cyclic AMP + H2O
-
Oryctolagus cuniculus 2'-AMP
-
?
nucleoside 2',3'-cyclic phosphate + H2O
-
Mus musculus nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O
-
Homo sapiens nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O
-
Rattus norvegicus nucleoside 2'-phosphate
-
?
nucleoside 2',3'-cyclic phosphate + H2O
-
Oryctolagus cuniculus nucleoside 2'-phosphate
-
?

Synonyms

Synonyms Comment Organism
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
Mus musculus
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
Homo sapiens
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
Rattus norvegicus
2',3'-cyclic nucleotide 3'-phosphodiesterase
-
Oryctolagus cuniculus
CNPase
-
Mus musculus
CNPase
-
Homo sapiens
CNPase
-
Rattus norvegicus
CNPase
-
Oryctolagus cuniculus

General Information

General Information Comment Organism
evolution the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms Mus musculus
evolution the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms Homo sapiens
evolution the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms Rattus norvegicus
evolution the catalytic domain is composed of about 240 amino acids, is highly conserved in mammals, and is present in all identified enzymes throughout different organisms Oryctolagus cuniculus
malfunction a C-terminally truncated variant of CNPase, as well as a mutant unable to membrane-associate, are affected in oligodendrocyte process outgrowth, formation and branching Mus musculus
malfunction changes in enzyme expression levels are linked to Alzheimer's disease, Down's syndrome, and catatonia-depression syndrome. A single-nucleotide polymorphism that does not alter the amino-acid sequence of the enzyme, but rather decreases its expression levels, has been suggested to play a role in schizophrenia Homo sapiens
malfunction truncations after amino acid 164 in recombinant rat enzyme result in a loss of phosphodiesterase activity Rattus norvegicus
additional information structure of the 2'-cyclic AM-bound enzyme active site and its catalytic mechanism, overview Mus musculus
additional information structure of the CNPase phosphodiesterase domain and its catalytic mechanism, overview Rattus norvegicus
physiological function in early stages of myelination, the enzyme is essential in oligodendrocyte process formation and branching, as well as for oligodendrocyte process outgrowth via its membrane association, as well as its ability to interact with the cytoskeleton. The role of CNPase after active myelination is related to axonal maintenance. Accumulation of 2',3'-cAMP is found in very young CNPase-deficient mice used to study traumatic brain injury, which develops post-traumatic axonal degeneration similar to that of older CNPase-deficient mice that do not experience brain trauma Mus musculus
physiological function the enzyme is possible auto-antigen in multiple sclerosis. CNPase isoform II is responsible for mitochondrial import, which is regulated via phosphorylation by protein kinase C. The mitochondrial, fully-processed isoform II does not drive morphological differentiation in cell cultures as isoform I does in oligodendrocytes. The enzyme, together with 2',3'-cAMP, is suggested to modulate the mitochondrial permeability transition, a proapoptotic event, in which Ca2+ is released from the mitochondrial matrix to the intermembrane space and cytoplasm Homo sapiens