Literature summary for 3.4.24.7 extracted from

Solomonov, I.; Zehorai, E.; Talmi-Frank, D.; Wolf, S.G.; Shainskaya, A.; Zhuravlev, A.; Kartvelishvily, E.; Visse, R.; Levin, Y.; Kampf, N.; Jaitin, D.A.; David, E.; Amit, I.; Nagase, H.; Sagi, I.
Distinct biological events generated by ECM proteolysis by two homologous collagenases (2016), Proc. Natl. Acad. Sci. USA, 113, 10884-10889 .

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression in bacterial cells	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	complete inhibition at 20 mM	Homo sapiens
EDTA	complete inhibition at 20 mM	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	the enzyme is secreted	Rattus norvegicus	-	-
extracellular matrix	-	Rattus norvegicus	31012	-

Metals/Ions

Metals/Ions	Comment	Organism
Ca2+	required	Homo sapiens
Ca2+	required	Rattus norvegicus
Zn2+	zinc metalloproteinase	Homo sapiens
Zn2+	zinc metalloproteinase	Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Collagen + H2O	Homo sapiens	-	?	-	?
Collagen + H2O	Rattus norvegicus	-	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P03956	-	-
Rattus norvegicus	B5DFD5	-	-

Purification (Commentary)

Purification (Comment)	Organism
solubilized and refolded recombinant enzyme by gel filtration and ultrafiltration	Homo sapiens

Renatured (Commentary)

Renatured (Comment)	Organism
recombinant enzyme from inclusion bodies is solubilized in denaturation buffer containing 50 mM Tris, pH 8.0, 20 mM DTT, 50 mM ZnCl2, 1 mM acetohydroxamic acid (AHA), and 8 M urea, stirred overnight at room temperature, followed by ultrafiltration and anion exchange chromatography. The enzyme is diluted in 20 mM Tris, pH 8.0, 20 mM cystamine, 6 M urea, and dialyzed against 5-8 l of 50 mM Tris, pH 8.0, 2 mM AHA, 1 mM hydroxyethyl sulfate, 4 M urea, 5 mM CaCl2 , 0.1 mM ZnCl2, 300 mM NaCl, 5 mM 2-mercaptoethanol, and 4 M urea at 4°C overnight with stirring. The last step of refolding is done twice, against 2 M urea, 50 mM Tris, pH 8.0, 10 mM CaCl2, 0.1 mM ZnCl2, 300 mM NaCl, and 2 mM AHA overnight, with stirring, at 4°C	Homo sapiens

Renatured (Comment)

Organism

recombinant enzyme from inclusion bodies is solubilized in denaturation buffer containing 50 mM Tris, pH 8.0, 20 mM DTT, 50 mM ZnCl2, 1 mM acetohydroxamic acid (AHA), and 8 M urea, stirred overnight at room temperature, followed by ultrafiltration and anion exchange chromatography. The enzyme is diluted in 20 mM Tris, pH 8.0, 20 mM cystamine, 6 M urea, and dialyzed against 5-8 l of 50 mM Tris, pH 8.0, 2 mM AHA, 1 mM hydroxyethyl sulfate, 4 M urea, 5 mM CaCl2 , 0.1 mM ZnCl2, 300 mM NaCl, 5 mM 2-mercaptoethanol, and 4 M urea at 4°C overnight with stirring. The last step of refolding is done twice, against 2 M urea, 50 mM Tris, pH 8.0, 10 mM CaCl2, 0.1 mM ZnCl2, 300 mM NaCl, and 2 mM AHA overnight, with stirring, at 4°C

Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	recombinant enzyme	Homo sapiens	-
fibroblast	-	Rattus norvegicus	-
additional information	detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts	Rattus norvegicus	-
Rat-1 cell	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
Collagen + H2O	-	Homo sapiens	?	-	?
Collagen + H2O	-	Rattus norvegicus	?	-	?
Collagen + H2O	natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13	Homo sapiens	?	-	?
Collagen + H2O	natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13. Cleavage sites identified in Col I-rich ECM under proteolytic degradation by MMP-1, overview	Rattus norvegicus	?	-	?
collagen type IV alpha2 + H2O	cleavage at sites L715 and T917	Homo sapiens	?	-	?
collagen type IV alpha2 + H2O	cleavage at sites L715 and T917	Rattus norvegicus	?	-	?
decorin + H2O	cleavage at site T310	Homo sapiens	?	-	?
decorin + H2O	cleavage at site T310	Rattus norvegicus	?	-	?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O	-	Homo sapiens	Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2	-	?
additional information	proteomic analysis of MMP-1 activity using LC-MS/MS analysis	Rattus norvegicus	?	-	?

Subunits

Subunits	Comment	Organism
More	tryptic peptide mapping in solution	Homo sapiens
More	tryptic peptide mapping in solution	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
matrix metalloproteinase-1	-	Rattus norvegicus
MMP-1	-	Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Homo sapiens
30	-	assay at	Rattus norvegicus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Homo sapiens
7.4	-	assay at	Rattus norvegicus

General Information

General Information	Comment	Organism
metabolism	the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes	Homo sapiens
metabolism	the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes	Rattus norvegicus
additional information	detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts, macrorheological properties and morphologies of natural and MMP-degraded ECMs	Rattus norvegicus
physiological function	the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview	Homo sapiens
physiological function	the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview	Rattus norvegicus