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Literature summary for 3.4.24.17 extracted from

  • Ceruso, M.; Howe, N.; Malthouse, J.P.
    Mechanism of the binding of Z-L-tryptophan and Z-L-phenylalanine to thermolysin and stromelysin-1 in aqueous solutions (2012), Biochim. Biophys. Acta, 1824, 303-310.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Z-L-tryptophan inhibits full length stromelysin_1-477 and truncated stromelysin_100-264, enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzyme binding, overview. The tryptophan side chain can bind in the S1 specificity site of stromelysin with the tryptophan alpha carboxylate group coordinated to the active site zinc atom Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the active site zinc atom of stromelysin-1 is replaced by cobalt Homo sapiens
Zn2+ metalloprotease Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P08254
-
-

Synonyms

Synonyms Comment Organism
stromelysin-1
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0063
-
Z-L-tryptophan pH 6.0, 25°C, recombinant full-length enzyme stromelysin1-477, enzyme contains Zn2+ Homo sapiens
0.021
-
Z-L-tryptophan pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens
0.03
-
Z-L-tryptophan pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Co2+ Homo sapiens
0.034
-
Z-L-tryptophan pH 5.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens
0.052
-
Z-L-tryptophan pH 7.1, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens

General Information

General Information Comment Organism
additional information the stromelysin-1 catalytic domain comprises residues 83-247 Homo sapiens