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Literature summary for 3.4.24.B9 extracted from

  • Koike, H.; Tomioka, S.; Sorimachi, H.; Saido, T.C.; Maruyama, K.; Okuyama, A.; Fujisawa-Sehara, A.; Ohno, S.; Suzuki, K.; Ishiura, S.
    Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein (1999), Biochem. J., 343, 371-375.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B9

Cloned(Commentary)

Cloned (Comment) Organism
expression of Sec-tagged wild-type and metalloprotease domain deletion mutant in COS-7 cells Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
metalloprotease inhibitor SI-27
-
 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane anchored Mus musculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ metalloprotease Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
proteins + H2O Mus musculus
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant from COS-7 cells Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid precursor protein + H2O alpha-secretase activity Mus musculus 90-100 kDa non-amyloid N-terminal protein fragment
-
 ?
proteins + H2O
-
 Mus musculus peptides
-
 ?

Synonyms

Synonyms Comment Organism
M12.209 Merops-ID Mus musculus
MDC9
-
 Mus musculus
meltrin-gamma
-
 Mus musculus

Temperature Optimum [°C]

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