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Results 1 - 10 of 14 > >>
EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12Eglin c very effective inhibitor Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12Eglin c - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12guanidine hydrochloride 1% residual activity in the presence of 4 mM guanidine hydrochloride Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12methoxysuccinyl-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 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12methoxysuccinyl-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 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12more - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12more mechanism Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12more 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 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12N-terminal 166 amino acid Pro region of alpha-lytic protease dual role of folding and inhibition Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.12N-Tert-butyloxycarbonylalanylpropylvaline boronic acid - Go to the Ligand Summary Page
Results 1 - 10 of 14 > >>