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Literature summary for 3.1.4.37 extracted from

  • Myllykoski, M.; Itoh, K.; Kangas, S.M.; Heape, A.M.; Kang, S.U.; Lubec, G.; Kursula, I.; Kursula, P.
    The N-terminal domain of the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: direct molecular interaction with the calcium sensor calmodulin (2012), J. Neurochem., 123, 515-524.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information no effect on enzyme activity by calmodulin binding Mus musculus
additional information no effect on enzyme activity by calmodulin binding Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type full-length enzyme and truncated mutants Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information generation of truncated enzyme mutants: CNP_20-398, CNP_25-398, CNP_20-420, CNP_20-185, and CNP_179-398, analysis of calmodulin binding activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
additional information no effect on enzyme activity by calmodulin binding Mus musculus
additional information no effect on enzyme activity by calmodulin binding Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Mus musculus 16020
-
membrane
-
Rattus norvegicus 16020
-
additional information the enzyme binds to calmodulin in a Ca2+-dependent manner via its binding site in the N-terminal domain, colocalization of CNPase and CaM during Schwann cell myelination in culture, molecular modeling Rattus norvegicus
-
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
isoform 2
-
Rattus norvegicus
-
isoform 2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein two phosphorylation sites on Tyr110 and Ser169 within the N-terminal domain Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type full-length enzyme and truncated mutants by nickel affinity chromatography and gel filtration or by calmodulin affinity chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Rattus norvegicus
-
CG-4 cell
-
Rattus norvegicus
-
dorsal root ganglion DRG explant cultures Mus musculus
-
myelin membrane the enzyme is a quantitatively major enzyme in myelin, where it localizes to the non-compact regions and is bound to the membrane surface Rattus norvegicus
-
Schwann cell myelinating, colocalization of CNPase and CaM during Schwann cell myelination in culture Rattus norvegicus
-

Synonyms

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

General Information

General Information Comment Organism
additional information role for the N-terminal domain of the enzyme in mediating multiple molecular interactions, molecular modeling, overview Mus musculus
additional information role for the N-terminal domain of the enzyme in mediating multiple molecular interactions, molecular modeling, overview Rattus norvegicus
physiological function the enzyme interacts with membrane surfaces, cytoskeletal proteins, and calmodulin Rattus norvegicus