Application | Comment | Organism |
---|---|---|
medicine | the understanding of the regulatory mechanisms that control the activity of the key proteinase in tumor cell invasion, is essential for the design of potent and safe anti-cancer therapies | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
MT1-MMP, lacking the C-terminal transmembrane and cytoplasmic domains, expression in Pichia pastoris | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | key protease in tumor cell invasion | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P50281 | cDNA fragment coding for peptide Ala21-Ser538 of the full-length MT1-MMP | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | trace amounts of active enzyme induce activation of the zymogen and its self-proteolysis. This autocatalytic processing generates six main forms of MT1-MMP. The enzyme functions as a self-convertase and is capable of cleaving its own prodomain at the furin cleavage motif RRKR-/-Y112, thus autocatalytically generating the mature MT1-MMP enzyme with an N-terminus starting at Tyr112. The mature enzyme undergoes further autocatalysis to the two distinct intermediates, N-terminus at Trp119 and at Asn130, and next to the three inactive ectodomain forms (N-terminus at Thr222, at Gly284, and at Thr299) | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | key protease in tumor cell invasion | Homo sapiens | ? | - |
? |