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Literature summary extracted from

  • Loechel, F.; Gilpin, B.J.; Engvall, E.; Albrechtsen, R.; Wewer, U.M.
    Human ADAM 12 (meltrin alpha) is an active metalloprotease (1998), J. Biol. Chem., 273, 16993-16997.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B10 transient expression in COS-7 cells of an enzyme mutant where the signal peptide, prodomain and metalloprotease domain are exchanged for an Ig kappa-chain leader sequence, secretion to the medium Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.B10 C179A site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain results in a no longer latent but inactive zymogen Homo sapiens
3.4.24.B10 C179S site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain results in a no longer latent but inactive zymogen Homo sapiens
3.4.24.B10 E351Q site-directed mutagenesis, exchange of the glutamic acid residue of the zinc binding domain involved in catalytic activity, inactive to form complexes with alpha2-macroglobulin Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B10 1,10-phenanthroline
-
 Homo sapiens
3.4.24.B10 EDTA complete inhibition Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B10 Zn2+ highly conserved zinc-binding motif HEXXHXXGXXH, the metalloprotease domain is the catalytically active site, the Met-turn is essential for the structural integrity of the zinc-binding site, Glu351 is essential for activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B10 68000
-
 x * 68000, processed recombinant mutant enzyme, SDS-PAGE, x * 92000, unprocessed recombinant mutant enzyme, SDS-PAGE Homo sapiens
3.4.24.B10 92000
-
 x * 68000, processed recombinant mutant enzyme, SDS-PAGE, x * 92000, unprocessed recombinant mutant enzyme, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B10 additional information Homo sapiens enzyme complexes alpha2-macroglobulin ?
-
 ?
3.4.24.B10 proteins + H2O Homo sapiens
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B10 Homo sapiens O43184
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B10 proteolytic modification the cysteine-switch of the prodomain maintaines the zymogen in a latent state, enzyme is synthesized as a catalytically inactive zymogen, in vivo cleavage by a furin-like endopeptidase, activation is chemically possible with N-ethylmaleimide, but not with Hg2+ Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B10 proteolysis of proteins the metalloprotease domain is catalytically active, Glu351 is essential for activity Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B10 additional information enzyme complexes alpha2-macroglobulin Homo sapiens ?
-
 ?
3.4.24.B10 protein + H2O
-
 Homo sapiens peptides
-
 ?
3.4.24.B10 proteins + H2O
-
 Homo sapiens peptides
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B10 ? x * 68000, processed recombinant mutant enzyme, SDS-PAGE, x * 92000, unprocessed recombinant mutant enzyme, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B10 a disintegrin and metalloproteinase domain 12
-
 Homo sapiens
3.4.24.B10 ADAM12
-
 Homo sapiens
3.4.24.B10 M12.212 Merops-ID Homo sapiens
3.4.24.B10 meltrin alpha
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B10 37
-
 alpha2-macroglobulin complexing assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B10 7.4
-
 alpha2-macroglobulin complexing assay at Homo sapiens