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Literature summary extracted from

  • Park, H.I.; Lee, S.; Ullah, A.; Cao, Q.; Sang, Q.X.
    Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker (2010), Anal. Biochem., 396, 262-268.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.B7 Brij-35 optimally activating at 0.056 mM, at concentrations above the critical micelle concentration, it inhibits the enzyme noncompetitively at 0.05%, i.e. 0.417 mM Homo sapiens
3.4.24.B7 additional information the hydrolytic activity of endometase is detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration of nonionic detergents tested, overview. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding site to impede catalysis Homo sapiens
3.4.24.B7 SDS optimally activating at 0.0095 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Tetradecyltrimethylammonium bromide optimally activating at 0.0075 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Triton X-100 optimally activating at 0.140 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Tween 20 optimally activating at 0.079 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.23 Brij-35 activates MMP-7 in a broad concentration range, but inhibits at high concentration Homo sapiens

Application

EC Number Application Comment Organism
3.4.24.B7 diagnostics MMP-26 is a putative early biomarker for human carcinomas Homo sapiens
3.4.24.23 diagnostics endometase is putative early biomarker for human carcinomas Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B7 expression of proMMP-26 in Escherichia coli in inclusion bodies Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B7 Brij-35 optimally activating at 0.056 mM, at concentrations above the critical micelle concentration, it inhibits the enzyme noncompetitively at 0.05%, i.e. 0.417 mM Homo sapiens
3.4.24.B7 additional information the hydrolytic activity of endometase is detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration of nonionic detergents tested, overview. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding site to impede catalysis Homo sapiens
3.4.24.B7 SDS optimally activating at 0.0095 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Tetradecyltrimethylammonium bromide optimally activating at 0.0075 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Triton X-100 optimally activating at 0.140 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.B7 Tween 20 optimally activating at 0.079 mM, at concentrations above the critical micelle concentration Homo sapiens
3.4.24.23 Brij-35 activates MMP-7 in a broad concentration range, but inhibits at high concentration Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B7 Ca2+ required Homo sapiens
3.4.24.23 Ca2+
-
Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B7 Homo sapiens
-
-
-
3.4.24.23 Homo sapiens P09237
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B7 proteolytic modification MMP-26 autoactivates Homo sapiens

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.4.24.B7 solubilization of recombinant proMMP-26 from Escherichia coli inclusion bodies by 8 M urea, followed by dialysis against 4 M urea, 1 mM DTT, and 50 mM HEPES or Tricine at pH 7.5 for at least 1 h, and then folded by dialysis against buffer containing 50 mM Hepes, 0.2 M, NaCl, 10 mM CaCl2, 20 lM ZnSO4, and 0.05% Brij-35 at pH 7.5 for 12 h three times, MMP-26 autoactivates Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.23 7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
-
Homo sapiens ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.24.B7 More the prodomain of MMP-26 is necessary for proper folding of the enzyme. Homology-modeling of the structure of the MMP-26 catalytic domain, overview Homo sapiens
3.4.24.23 More MMP-7 possesses hydrophobic surface areas around the catalytic site, PDB code 2DDY Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B7 endometase
-
Homo sapiens
3.4.24.B7 matrilysin 2
-
Homo sapiens
3.4.24.B7 MMP-26
-
Homo sapiens
3.4.24.23 matrilysin
-
Homo sapiens
3.4.24.23 MMP-7
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B7 25
-
assay at Homo sapiens
3.4.24.23 25
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B7 7.5
-
assay at Homo sapiens
3.4.24.23 7.5
-
assay at Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.B7 additional information
-
additional information detergent inhibition kinetics, overview Homo sapiens
3.4.24.B7 0.24
-
Brij-35 pH 7.5, 25°C Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.24.B7 0.079
-
pH 7.5, 25°C Homo sapiens Tetradecyltrimethylammonium bromide
3.4.24.B7 0.11
-
pH 7.5, 25°C Homo sapiens SDS
3.4.24.B7 0.56
-
pH 7.5, 25°C Homo sapiens Brij-35
3.4.24.B7 0.64
-
pH 7.5, 25°C Homo sapiens Tween 20
3.4.24.B7 1.3
-
pH 7.5, 25°C Homo sapiens Triton X-100
3.4.24.23 4.6
-
pH 7.5, 25°C Homo sapiens Brij-35

General Information

EC Number General Information Comment Organism
3.4.24.B7 additional information under physiological conditions, a lipid or membrane microenvironment may regulate enzymatic activity Homo sapiens