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Literature summary for 3.1.4.37 extracted from

  • Myllykoski, M.; Kursula, P.
    Expression, purification, and initial characterization of different domains of recombinant mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase, an enigmatic enzyme from the myelin sheath (2010), BMC Res. Notes, 3, 12.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
subcloned into pTH27, expressed in Escherichia coli Rosetta (DE3) with a TEV protease-cleavable His-tag Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.537
-
2',3'-cAMP full-length protein Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ assay buffer Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26700
-
x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase Mus musculus
45200
-
x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni-affinity chromatography followed by gel filtration Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
myelin sheath
-
Mus musculus
-

Storage Stability

Storage Stability Organism
4°C, for weeks Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cAMP + H2O 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 Mus musculus 2'-AMP
-
?

Subunits

Subunits Comment Organism
? x * 26700, SDS-PAGE, C-terminal domain. x * 45200, SDS-PAGE, full-length CNPase Mus musculus

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65 75 increase in the melting temperature induced by both pH 5.5 and high salt concentration. At pH 5.5, without NaCl: ca. 68°C and with 500 mM NaCl: ca. 75°C. At pH 7.5 without NaCl and with 500 mM NaCl: ca. 70°C Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
118
-
2',3'-cAMP full-length protein Mus musculus

pH Stability

pH Stability pH Stability Maximum Comment Organism
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 Mus musculus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
220
-
2',3'-cAMP full-length protein Mus musculus