Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | activation of enzyme by proteolytic cleaveage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal fragment. In solution, the fragment is still a potent inhibitor of enzyme activity. Amino acids D273 and D275 are essential for inhibitory effect. Peptide 265-285 increases the Km-value for NAD. Two-site binding model for inhibition | Lysinibacillus sphaericus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0403 | - |
NAD+ | pH 7.4, absence of peptide 265-285 | Lysinibacillus sphaericus | |
1.133 | - |
NAD+ | pH 7.4, presence of peptide 265-285 | Lysinibacillus sphaericus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lysinibacillus sphaericus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | activation of enzyme by proteolytic cleavage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal inhibitory fragment | Lysinibacillus sphaericus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
soy bean trypsin inhibitor + NAD+ | - |
Lysinibacillus sphaericus | nicotinamide + ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.2 | - |
NAD+ | pH 7.4, absence of peptide 265-285 | Lysinibacillus sphaericus | |
10.6 | - |
NAD+ | pH 7.4, presence of peptide 265-285 | Lysinibacillus sphaericus |