Literature summary for 3.4.24.80 extracted from

Cerofolini, L.; Amar, S.; Lauer, J.L.; Martelli, T.; Fragai, M.; Luchinat, C.; Fields, G.B.
Bilayer membrane modulation of membrane type 1 matrix metalloproteinase (MT1-MMP) structure and proteolytic activity (2016), Sci. Rep., 6, 29511 .

Search for more literature for 3.4.24.80

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS in inclusion bodies	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E240A	site-directed mutagenesis, inactive enzyme mutant	Homo sapiens
S466P	site-directed mutagenesis	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Homo sapiens	9986	-
membrane	-	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc-dependent endopeptidase, enzyme inactivation by removal of the active site Zn2+ by dialysis	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P50281	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	MT1-MMP is activated by incubation of pro-sMT1-MMP with rhtrypsin-3 and cleavage of the propeptide	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
solubilized recombinant wild-type and mutant enzymes from Escherichia coli strain Rosetta(DE3)pLysS	Homo sapiens

Renatured (Commentary)

Renatured (Comment)	Organism
recombinant enzymes from Escherichia coli inclusion bodies by three steps of dialysis in buffer 1 containing 1.5 M urea, 50 mM Tris, pH 8, 150 mM NaCl, 5 mM CaCl2, 0.1 mM ZnCl2, 5 mM 2-mercaptoethanol, 1 mM 2-hydroxyethyl disulphide, 0.1% Brij 35 v/v, and 1 mM PMSF, or in buffer 2 containing 50 mM Tris, pH 8, 150 mM NaCl, 5 mM CaCl2, 0.05 mM ZnCl2, 5 mM 2-mercaptoethanol, 1 mM 2-hydroxyethyl disulphide, 0.1% Brij 35 v/v, and 1 mM PMSF, or in buffer 3 containing 50 mM Tris, pH 8.0, 150 mM NaCl, 5 mM CaCl2, 0.05 mM ZnCl2, 0.1% Brij 35 v/v, and 1 mM PMSF	Homo sapiens

Renatured (Comment)

Organism

recombinant enzymes from Escherichia coli inclusion bodies by three steps of dialysis in buffer 1 containing 1.5 M urea, 50 mM Tris, pH 8, 150 mM NaCl, 5 mM CaCl2, 0.1 mM ZnCl2, 5 mM 2-mercaptoethanol, 1 mM 2-hydroxyethyl disulphide, 0.1% Brij 35 v/v, and 1 mM PMSF, or in buffer 2 containing 50 mM Tris, pH 8, 150 mM NaCl, 5 mM CaCl2, 0.05 mM ZnCl2, 5 mM 2-mercaptoethanol, 1 mM 2-hydroxyethyl disulphide, 0.1% Brij 35 v/v, and 1 mM PMSF, or in buffer 3 containing 50 mM Tris, pH 8.0, 150 mM NaCl, 5 mM CaCl2, 0.05 mM ZnCl2, 0.1% Brij 35 v/v, and 1 mM PMSF

Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
((Gly-Pro-4-hydroxyproline)5-Gly-Pro-Lys(7-methoxycoumarin-4-yl) acetyl)-Gly-Pro-Gln-Gly-Cys(4-methoxybenzyl)-Arg-Gly-Gln-Lys(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-4-hydroxyproline)5-NH2 + H2O	triple-helical substrate fTHP-9	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	enzyme MT1-MMP possesses a multidomain structure, encompassing a signal peptide, propeptide, catalytic (CAT) domain, hinge region (linker 1), hemopexin-like (HPX) domain, stalk region (linker 2), transmembrane domain (TM), and cytoplasmic tail (CT)	Homo sapiens

Synonyms

Synonyms	Comment	Organism
membrane type 1 matrix	-	Homo sapiens
metalloproteinase	-	Homo sapiens
MT1-MMP	-	Homo sapiens
pericellular collagenase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	a single mutation in the putative membrane interaction region of MT1-MMP (Ser466Pro) results in lower enzyme activation by bicelles	Homo sapiens
additional information	an initial structural framework defines the role(s) of cell membranes in modulating proteolysis. Examination of simultaneous membrane interaction and triple-helix binding reveals a possible regulation of proteolysis due to steric effects of the membrane. Activity analysis of MT1-MMP in membrane-like environments, Interaction of the isolated 15N MT1-MMP HPX domain with bilayers, with a collagen-like triple helical peptide (THP) alone or in the presence of bicelles, or with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), interaction of 15N sMT1-MMP with bicelles, NMR spectroscopic analysis, modelling, overview	Homo sapiens
physiological function	membrane type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane cell-surface protease that has been implicated in numerous pathologies. The pericellular collagenase membrane-type 1 matrix metalloproteinase (MT1-MMP) and membrane-mimicking environments interplay in substrate binding and processing. MT1-MMP transiently associates with bicelles and cells through distinct residues in blades III and IV of its hemopexin-like domain, while binding of collagen-like triple helices occurs within blades I and II of this domain. MT1-MMP collagenolytic activity appears critical for transmigration of tumor cells, endothelial cells, and fibroblasts through collagen matrices, while post-myocardial infarction survival has been correlated to the collagenolytic potential of cardiac fibroblasts, where MT1-MMP is the dominant collagenase within myocardial tissues	Homo sapiens