Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli K12 strain JM109 and secretion to the cell culture medium | Bacillus thermoproteolyticus |
Protein Variants | Comment | Organism |
---|---|---|
E143A | site-directed mutagenesis, E143A might exist as a complex with the propetide in the supernatant, inactive mutant, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
additional information | a mutant thermolysin is affected by its autocatalytic digestion activity | Bacillus thermoproteolyticus |
N112A | site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
N112D | site-directed mutagenesis, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
N112E | site-directed mutagenesis, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
N112H | site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
N112K | site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
N112R | site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected | Bacillus thermoproteolyticus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
TMP1 | - |
Bacillus thermoproteolyticus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Bacillus thermoproteolyticus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | four ions per enzyme molecule required for stability | Bacillus thermoproteolyticus | |
Zn2+ | zinc metalloproteinase, one ion per enzyme molecule required for activity | Bacillus thermoproteolyticus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
26000 | - |
x * 22 852, propeptide of thermolysin, sequence calculation, x * 26000, mature enzyme, SDS-PAGE | Bacillus thermoproteolyticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thermoproteolyticus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | thermolysin is synthesized as inactive pre-proenzyme and receives autocatalytic cleavage of the peptide bond linking the pro- and mature sequences, overview | Bacillus thermoproteolyticus |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli K12 strain JM109 by hydrophobic interaction and Gly-D-Phe affinity chromatography | Bacillus thermoproteolyticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? | |
additional information | thermolysin is a thermostable neutral metalloproteinase and performs autocatalytic cleavage for pro-enzyme activation | Bacillus thermoproteolyticus | ? | - |
? | |
N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? | |
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O | i.e. FAGLA | Bacillus thermoproteolyticus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 22 852, propeptide of thermolysin, sequence calculation, x * 26000, mature enzyme, SDS-PAGE | Bacillus thermoproteolyticus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus thermoproteolyticus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7 | - |
Bacillus thermoproteolyticus |