Application | Comment | Organism |
---|---|---|
synthesis | introduction of ionizing residues into the active site of enzyme as a means of modifying its pH-activity profile | Bacillus thermoproteolyticus |
Protein Variants | Comment | Organism |
---|---|---|
N112A | no enzymic activity in supernatant of cells expressing mutant | Bacillus thermoproteolyticus |
N112D | supernatants of cells expressing mutant show 18% of wild-type activity | Bacillus thermoproteolyticus |
N112E | supernatants of cells expressing mutant show 5% of wild-type activity | Bacillus thermoproteolyticus |
N112H | no enzymic activity in supernatant of cells expressing mutant | Bacillus thermoproteolyticus |
N112K | no enzymic activity in supernatant of cells expressing mutant | Bacillus thermoproteolyticus |
N112R | no enzymic activity in supernatant of cells expressing mutant | Bacillus thermoproteolyticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thermoproteolyticus | P00800 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O | - |
Bacillus thermoproteolyticus | N-carbobenzoxy-L-Asp + L-Phe-methyl ester | - |
? | |
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O | - |
Bacillus thermoproteolyticus | ? | - |
? |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8.5 | for hydrolysis of neutral substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide, wild-type and mutants N112D, N112E exhibit bell-shaped pH-dependence. For hydrolysis of negatively charged substrate N-carbobenzoxy-L-Asp-L-Phe methyl ester, wild-type shows bell-shaped pH-dependence, for mutants N112D and N112E, pH-dependence of the ratio kcat/Km decreases with increase in pH from 5.5 to 8.5 | Bacillus thermoproteolyticus |