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Literature summary for 3.4.24.63 extracted from

  • Sato, Y.; Kobayashi, D.; Kohno, T.; Kidani, Y.; Prox, J.; Becker-Pauly, C.; Hattori, M.
    Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage (2015), J. Biochem., 159, 305-312 .
    View publication on PubMed
Search for more literature for 3.4.24.63

Cloned(Commentary)

Cloned (Comment) Organism
gene MEP1B, recombinant enzyme expression in COS-7 and HEK293T cells Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
actinonin
-
 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Mus musculus 9986
-
membrane
-
 Mus musculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metalloprotease Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Reelin + H2O Mus musculus Reelin is a secreted glycoprotein whose function is regulated by proteolysis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q61847
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
neuron cerebellar granular neurons Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Reelin + H2O Reelin is a secreted glycoprotein whose function is regulated by proteolysis Mus musculus ?
-
 ?
Reelin + H2O cleavage between Ala2688 and Asp2689, the specific cleavage site of Reelin called C-t is located approximately between the sixth and seventh Reelin repeat Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
meprin beta
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

General Information

General Information Comment Organism
physiological function actinonin, a meprin alpha (EC 3.4.24.18) and meprin beta inhibitor, does not inhibit the Reelin-cleaving activity of cerebellar granular neurons (CGN) and the amount of Reelin fragments in brains of meprin beta knock-out mice is not significantly different from that of the wild-type, indicating that meprin beta does not play a major role in Reelin cleavage under basal conditions. Meprin alpha and meprin beta probably join the modulators of Reelin signalling as they cleave Reelin at a specific site and are upregulated under specific pathological conditions Mus musculus