Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Inhibitors Comment Organism Structure
3.4.24.17 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
3.4.24.27 2-phenylpropionyl-L-phenylalanine
-
 Bacillus sp. (in: Bacteria)
3.4.24.27 2-phenylpropionyl-Leu-Trp
-
 Bacillus sp. (in: Bacteria)
3.4.24.27 beta-phenylpropionyl-L-phenylalanine
-
 Bacillus thermoproteolyticus
3.4.24.27 additional information the active site zinc atom is tetrahedrally coordinated when the inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine are bound to thermolysin. pH dependencies of inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine and binding to thermolysin, detailed overview Bacillus sp. (in: Bacteria)
3.4.24.27 N-Benzyloxycarbonyl-L-phenylalanine binding mechanism in aqueous solution, NMR and spectrophotometric analysis, overview. Substitution of Zn2+ by Co2+ decreases the binding affinity of the inhibitor, overview Bacillus sp. (in: Bacteria)
3.4.24.27 N-benzyloxycarbonyl-L-tryptophan binding mechanism in aqueous solution, NMR and spectrophotometric analysis, overview. Substitution of Zn2+ by Co2+ decreases the binding affinity of the inhibitor, overview. With thermolysin, a 1 M concentration of NaSCN produces an 2fold increase in its Ki value from 0.087 mM to 0.19 mM for the inhibitor N-benzyloxycarbonyl-tryptophan Bacillus sp. (in: Bacteria)
3.4.24.27 P-Leu-Trp
-
 Bacillus thermoproteolyticus
3.4.24.27 phosphoramidon
-
 Bacillus sp. (in: Bacteria)
3.4.24.27 phosphoramidon
-
 Bacillus thermoproteolyticus
3.4.24.27 Z-L-phenylalanine enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzyme binding, overview. The carbobenzyloxyl protecting group and not the phenylalanyl phenyl group that is bound in the S1' specificity pocket and the alpha carboxylate group is directly coordinated to the active site zinc atom Bacillus thermoproteolyticus
3.4.24.27 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 enzym ebinding, 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. L-tryptophan binds equally strongly to zinc or cobalt substituted thermolysin Bacillus thermoproteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.17 Co2+ the active site zinc atom of stromelysin-1 is replaced by cobalt Homo sapiens
3.4.24.17 Zn2+ metalloprotease Homo sapiens
3.4.24.27 Ca2+ required Bacillus sp. (in: Bacteria)
3.4.24.27 Co2+ the active site zinc atom of thermolysin is replaced by cobalt Bacillus thermoproteolyticus
3.4.24.27 NaSCN 3fold increase in catalytic activity of thermolysin when the NaSCN concentration is increased to 1 M, but decrease in catalytic activity at higher concentrations of NaSCN Bacillus sp. (in: Bacteria)
3.4.24.27 Zn2+ metalloprotease Bacillus thermoproteolyticus
3.4.24.27 Zn2+ dependent on, thermolysin is a bacterial zinc metalloproteinase. The active site zinc atom is tetrahedrally coordinated when the inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine are bound to thermolysin Bacillus sp. (in: Bacteria)

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.17 Homo sapiens P08254
-
-
3.4.24.27 Bacillus sp. (in: Bacteria)
-
-
-
3.4.24.27 Bacillus thermoproteolyticus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.27 commercial preparation
-
 Bacillus sp. (in: Bacteria)
-
3.4.24.27 commercial preparation enzyme crystals Bacillus thermoproteolyticus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.27 9340
-
 pH and temperature not specified in the publication Bacillus thermoproteolyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.27 N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
-
 Bacillus sp. (in: Bacteria) N-[3-(2-furyl)acryloyl]-glycine + L-leucine amide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.17 stromelysin-1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.17 25
-
 assay at Homo sapiens
3.4.24.27 25
-
 assay at Bacillus thermoproteolyticus
3.4.24.27 37
-
 assay at Bacillus sp. (in: Bacteria)

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.17 6
-
-
 Homo sapiens
3.4.24.27 7 7.5 assay at Bacillus sp. (in: Bacteria)
3.4.24.27 7
-
-
 Bacillus thermoproteolyticus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.17 0.0063
-
 Z-L-tryptophan pH 6.0, 25°C, recombinant full-length enzyme stromelysin1-477, enzyme contains Zn2+ Homo sapiens
3.4.24.17 0.021
-
 Z-L-tryptophan pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens
3.4.24.17 0.03
-
 Z-L-tryptophan pH 6.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Co2+ Homo sapiens
3.4.24.17 0.034
-
 Z-L-tryptophan pH 5.0, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens
3.4.24.17 0.052
-
 Z-L-tryptophan pH 7.1, 25°C, recombinant truncated enzyme stromelysin1-264, enzyme contains Zn2+ Homo sapiens
3.4.24.27 0.000015
-
 2-phenylpropionyl-Leu-Trp pH 7.2, temperature not specified in the publication Bacillus sp. (in: Bacteria)
3.4.24.27 0.000015
-
 P-Leu-Trp pH 7.2, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 0.00003
-
 phosphoramidon pH 7.2, temperature not specified in the publication Bacillus sp. (in: Bacteria)
3.4.24.27 0.00003
-
 phosphoramidon pH 7.2, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 0.007
-
 N-benzyloxycarbonyl-L-tryptophan pH 5.0, 37°C, Co2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.007
-
 Z-L-tryptophan pH 5.0, 25°C, enzyme contains Co2+ Bacillus thermoproteolyticus
3.4.24.27 0.008
-
 N-Benzyloxycarbonyl-L-phenylalanine pH 5.0, 37°C, Co2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.008
-
 N-benzyloxycarbonyl-L-tryptophan pH 5.0, 37°C, Zn2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.008
-
 Z-L-phenylalanine pH 5.0, 25°C, enzyme contains Co2+ Bacillus thermoproteolyticus
3.4.24.27 0.008
-
 Z-L-tryptophan pH 5.0, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 0.012
-
 N-Benzyloxycarbonyl-L-phenylalanine pH 5.1, 37°C, Zn2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.012
-
 Z-L-tryptophan pH 5.1, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 0.019
-
 Z-L-tryptophan pH 5.0, 25°C, enzyme contains Zn2+, presence of 1 M NaSCN Bacillus thermoproteolyticus
3.4.24.27 0.021
-
 Z-L-tryptophan pH 5.0, 25°C, enzyme contains Co2+, presence of 1 M NaSCN Bacillus thermoproteolyticus
3.4.24.27 0.087
-
 N-benzyloxycarbonyl-L-tryptophan pH 7.0, 37°C, Zn2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.087
-
 Z-L-tryptophan pH 7.0, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 0.16
-
 N-Benzyloxycarbonyl-L-phenylalanine pH 7.1, 37°C, Co2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.16
-
 Z-L-phenylalanine pH 7.1, 25°C, enzyme contains Co2+ Bacillus thermoproteolyticus
3.4.24.27 0.19
-
 N-benzyloxycarbonyl-L-tryptophan pH 7.0, 37°C, Zn2+-bound enzyme, in presence of 1 M NaSCN Bacillus sp. (in: Bacteria)
3.4.24.27 0.21
-
 N-benzyloxycarbonyl-L-tryptophan pH 7.0, 37°C, Co2+-bound enzyme, in presence of 1 M NaSCN Bacillus sp. (in: Bacteria)
3.4.24.27 0.37
-
 N-Benzyloxycarbonyl-L-phenylalanine pH 7.0, 37°C, Zn2+-bound enzyme Bacillus sp. (in: Bacteria)
3.4.24.27 0.37
-
 Z-L-phenylalanine pH 7.0, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus
3.4.24.27 1.6
-
 2-phenylpropionyl-L-phenylalanine pH 8.6, temperature not specified in the publication Bacillus sp. (in: Bacteria)
3.4.24.27 1.6
-
 beta-phenylpropionyl-L-phenylalanine pH 6.8, 25°C, enzyme contains Zn2+ Bacillus thermoproteolyticus

General Information

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