Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.18 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

Cloned(Commentary)

Cloned (Comment) Organism
gene MEP1A, 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
extracellular
-
Mus musculus
-
-

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 P28825
-
-

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.
additional information meprin alpha, but not meprin beta, cleaves Reelin in which Asp2689 is replaced with Lys (Reelin-DK mutant) Mus musculus ?
-
?
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 alpha
-
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 and meprin beta (EC 3.4.24.63) 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