EC Number |
Inhibitors |
Structure |
---|
3.4.21.12 | Eglin c |
very effective inhibitor |
|
3.4.21.12 | Eglin c |
- |
|
3.4.21.12 | guanidine hydrochloride |
1% residual activity in the presence of 4 mM guanidine hydrochloride |
|
3.4.21.12 | methoxysuccinyl-Ala-Ala-Pro-L-boroPhe |
the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates close to tetrahedral boron coordination in the active site of the enzyme/inhibitor complex |
|
3.4.21.12 | methoxysuccinyl-Ala-Ala-Pro-L-boroVal |
the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates tetrahedral boron coordination in the active site of the enzyme/inhibitor complex |
|
3.4.21.12 | more |
- |
|
3.4.21.12 | more |
mechanism |
|
3.4.21.12 | more |
lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity |
|
3.4.21.12 | N-terminal 166 amino acid Pro region of alpha-lytic protease |
dual role of folding and inhibition |
|
3.4.21.12 | N-Tert-butyloxycarbonylalanylpropylvaline boronic acid |
- |
|