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Literature summary for 3.1.4.37 extracted from

  • Myllykoski, M.; Raasakka, A.; Han, H.; Kursula, P.
    Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation (2012), PLoS ONE, 7, e32336.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.37

Crystallization (Commentary)

Crystallization (Comment) Organism
phosphodiesterase domain of the enzyme with bound citrate, sulfate, NADP+, and 2-AMP, mixing of protein in 10 mM sodium citrate pH 5.5, 50 mM NaCl, 10% glycerol, and 1 mM DTT, with crystallization solution, X-ray diffraction structure determination and analysis at 1.74-2.4 A resolution, molecular replacement and modeling. Crystallization is only successful with sulfate or citrate present Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
sulfate two sulfate molecules are located in the vicinity of the catalytic site, the active-site sulfate mimics the substrate phosphate group and interacts with all 4 conserved residues of the two HxTx motifs and the two central water molecules in the catalytic site through H-bonds, being also in contact with the backbone carbonyl of Pro320 and bulk solvent. The second sulfate stabilizes the long alpha6-beta5 loop Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 monomeric enzyme, light scattering and refractive index Mus musculus
78000
-
 dimeric enzyme, light scattering and refractive index Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nucleoside 2',3'-cyclic phosphate + H2O Mus musculus
-
 nucleoside 2'-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P16330
-
-

Reaction

Reaction Comment Organism Reaction ID
nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 2'-phosphate catalytic mechanism Mus musculus
a

Source Tissue

Source Tissue Comment Organism Textmining
myelin membrane a highly abundant membrane-associated enzyme in the myelin sheath of the vertebrate nervous system Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cyclic AMP + H2O product binding structure, overview Mus musculus 2'-AMP
-
 ?
nucleoside 2',3'-cyclic phosphate + H2O
-
 Mus musculus nucleoside 2'-phosphate
-
 ?

Subunits

Subunits Comment Organism
monomer or dimer monomer-dimer equilibrium for full-length enzyme, dimerization is possibly mediated by the N-terminal domain Mus musculus

Synonyms

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

General Information

General Information Comment Organism
evolution the enzyme is a unique member of the 2H phosphoesterase family. Large differences in the active-site vicinity are observed when comparing more distant members of the 2H family Mus musculus
additional information binding mode of nucleotide ligands in the active site, structure-function analysis, catalytic mechanism, overview. Flexible loops might play roles in substrate recognition. The enzyme's N-terminal domain is involved in RNA binding and dimerization Mus musculus