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Literature summary extracted from

  • Loechel, F.; Overgaard, M.T.; Oxvig, C.; Albrechtsen, R.; Wewer, U.M.
    Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch (1999), J. Biol. Chem., 274, 13427-13433.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B10 transient expression in COS-7 cells of the enzyme mutants, 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, still active in complex formation with alpha2-macroglobulin Homo sapiens
3.4.24.B10 C179H site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain, still active in complex formation with alpha2-macroglobulin Homo sapiens
3.4.24.B10 C179H/E351Q 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 the glutamic acid residue and of the zinc binding domain involved in catalytic activity, inactive to form complexes with alpha2-macroglobulin, results in a no longer latent but inactive zymogen Homo sapiens
3.4.24.B10 additional information KR207NG mutation prevents cleavage of the prodomain by furin, construction of enzyme mutants where the prodomain or the metalloprotease domain or both are eliminated or exchanged for an Ig kappa-chain leader sequence, secretion to the medium, inactive mutant Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B10 1,10-phenanthroline
-
 Homo sapiens
3.4.24.B10 hydroxamate inhibitor BB-94 slight inhibition Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B10 Zn2+ metalloprotease domain is the catalytically active site 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 protein + 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 glycoprotein degylcosylation with endoglycosidase H Homo sapiens
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, autoactivation is possible with N-ethylmaleimide Homo sapiens

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
-
 ?

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
-
 assay at Homo sapiens

pH Optimum

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