EC Number | General Stability | Organism |
---|---|---|
3.2.1.132 | heat treatment leads at a concentration of 0.0106 mM protein at 75°C to a irreversible unfolding, but this is reversible when the protein concentation is 20 times lower | Bacillus subtilis |
3.2.1.132 | unfolding and refolding kinetics with urea are both monophasic half-life for unfolding in 6 M urea is 78.8 s and in 1.75 M urea 73.7 s | Bacillus subtilis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.132 | extracellular | - |
Bacillus subtilis | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.132 | Ca2+ | influences folding an stability of newly translocated protein, one weak Ca2+-binding site with a KA of 300 M-1 | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.132 | chitosan + H2O | Bacillus subtilis | - |
? | - |
? | |
3.2.1.132 | chitosan + H2O | Bacillus subtilis GM9804 | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.132 | Bacillus subtilis | - |
GM9804 | - |
3.2.1.132 | Bacillus subtilis GM9804 | - |
GM9804 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.132 | chitosan + H2O | - |
Bacillus subtilis | ? | - |
? | |
3.2.1.132 | chitosan + H2O | - |
Bacillus subtilis GM9804 | ? | - |
? |