Literature summary for 3.4.24.80 extracted from

Rozanov, D.V.; Strongin, A.Y.
Membrane Type-1 Matrix metalloproteinase functions as a proprotein self-convertase (2003), J. Biol. Chem., 278, 8257-8260.

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Application

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(Commentary)

Cloned (Comment)	Organism
MT1-MMP, lacking the C-terminal transmembrane and cytoplasmic domains, expression in Pichia pastoris	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	key protease in tumor cell invasion	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P50281	cDNA fragment coding for peptide Ala21-Ser538 of the full-length MT1-MMP	-

Posttranslational Modification

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	key protease in tumor cell invasion	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)