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3.4.24.80: membrane-type matrix metalloproteinase-1

This is an abbreviated version!
For detailed information about membrane-type matrix metalloproteinase-1, go to the full flat file.

Word Map on EC 3.4.24.80

Reaction

endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-/-Leu. Other bonds hydrolysed include Gly35-/-Ile in the propeptide of collagenase 3, and Asn341-/-Phe, Asp441-/-Leu and Gln354-/-Thr in the aggrecan interglobular domain =

Synonyms

ectMMP-14, gelatinase A, interstitial MT1-MMP, matrix metalloprotease 14, matrix metalloproteinase 14, matrix metalloproteinase MT 1, matrix metalloproteinase MT-MMP-1, matrix metalloproteinase MT1-MMP, matrix metalloproteinase-14, membrane type 1 matrix, membrane type 1 matrix metalloproteinase, membrane type 1 MMP, membrane type 1-matrix metalloproteinase, membrane type 1-MMP, membrane type I MMP, membrane type matrix metalloproteinase, membrane type MMP-1, membrane type MT1-MMP, membrane type-1 matrix metalloprotease, membrane type-1 matrix metalloprotease 1, membrane type-1 matrix metalloproteinase, membrane type-1 MMP, membrane type-I matrix metalloproteinase, membrane type-I MMP, membrane-anchored matrix metalloproteinase 14, membrane-type 1 matrix metalloproteinase, membrane-type 1 matrix metalloproteinase 1, membrane-type 1 MMP, membrane-type 1-matrix metalloproteinase, membrane-type I matrix metalloproteinase, membrane-type matrix metalloproteinase MT1-MMP, membrane-type matrix metalloproteinase-1, membrane-type metalloproteinase MT1-MMP, membrane-type MMP, metalloproteinase, MMP-14, MMP-2, MMP-8, MMP14, mmp14a, mmp14b, More, MT-MMP-1, MT-MMP1, MT1-MMP, MT1-MMP/MMP-14, MT1-MPP, MTI-MMP, pericellular collagenase, proteinase, matrix metallo-, sMT1-MMP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.80 membrane-type matrix metalloproteinase-1

Renatured

Renatured on EC 3.4.24.80 - membrane-type matrix metalloproteinase-1

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dialysis against a 10fold volume of 50 mM Tris-HCl pH 8.5, 100 mM NaCl, 10 mM CaCl2, 10 mM zinc acetate, and 2 M urea
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
refolding of the purified polypeptide to active enzyme by gradient dialysis with urea gradient from 6 M decreasing to 0 M and 2-mercaptoethanol gradient from 150 mM decreasing to 0 mM in the presence of CaCl2 and ZnCl2