General Stability | Organism |
---|---|
Substrate binding stabilizes the enzyme | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the temperature dependence of the kinetics and thermodynamic parameters suggest that the enzyme exists in two, i.e. cold and hot forms, at 22°C the cold form turns into the hot one possibly owing to a conformational change | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Bacillus subtilis 72 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues | Bacillus subtilis | ? | - |
? | |
additional information | influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues | Bacillus subtilis 72 | ? | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
stable below | Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Bacillus subtilis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5.5 | 9 | stable | Bacillus subtilis |