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Literature summary for 3.4.24.80 extracted from

  • Koo, H.M.; Kim, J.H.; Hwang, I.K.; Lee, S.J.; Kim, T.H.; Rhee, K.H.; Lee, S.T.
    Refolding of the catalytic and hinge domains of human MT1-MMP expressed in Escherichia coli and its characterization (2002), Mol. Cell, 13, 118-124.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
catalytic and hinge domain Homo sapiens

Protein Variants

Protein Variants Comment Organism
E240A polypeptide can not be refolded Homo sapiens
K110A processing of the enzyme is blocked Homo sapiens
R108A processing of the enzyme is blocked Homo sapiens
R111A processing of the enzyme is blocked Homo sapiens
Y112F normal enzyme processing Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00344
-
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 pH 7.5, 37°C, mature and mutant enzyme Homo sapiens

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
catalytic and hinge domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P50281
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O fluorescent peptide Homo sapiens ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens