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Results 1 - 10 of 83 > >>
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EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(1R,3S,4R,7R,8S)-3-hydroxymethyl-2,6-dioxa-bicyclo-[2.2.2]-octane-7,8-diol 17% inhibition at 4 mM Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2R,3S,4S,5S,2'R,3'S,4'S,5'S)-2,2'-butane-1,4-diylbis[5-[(1S)-1,2-dihydroxyethyl]-3,4-dihydroxypyrrolidinium] dichloride - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2S)-2-deoxy-2-selenonium-2-[(2S,3S,4R,5S)-2,3,4,5,6-pentahydroxyhexyl]-D-arabinitol chloride a transition-state analogue, shows about 25% inhibition at 0.5 mm Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2S)-2-deoxy-2-sulfonium-2-[(2S,3S,4R,5S)-2,3,4,5,6-pentahydroxyhexyl]-D-arabinitol chloride a transition-state analogue, shows about 25% inhibition at 0.5 mm Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2S,3S,4S,5R)-2-[(1S)-1,2-dihydroxyethyl]-5-propylpyrrolidine-3,4-diol - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2S,3S,4S,5R)-2-[(1S)-1,2-dihydroxyethyl]-5-[(1E)-prop-1-en-1-yl]pyrrolidine-3,4-diol - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0053 mM, comparison with inhibition of Klebsiella pneumoniae enzyme Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(4-chlorophenyl)(1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-4-yl)methanone i.e. MS-208, a non-substrate-like inhibitor, mixed inhibition due to a lack of direct competition between MS-208 and the enzyme substrate. Molecular dynamics studies reveal that the MS-208 inhibition occurs by preventing complete closure of an active site mobile loop that is necessary for productive substrate binding. The results suggest the presence of an A-site with potential druggability. Kinetic analysis, docking, and molecular dynamics simulation and modeling of enzyme binding, overview. Model of the tertiary complex MtUGM:UDP-Galp:MS-208. Two A-loop residues, Glu321 and Asp322, are stabilized by MS-208 binding yet destabilized by UDP-Galp binding, with the former effect being more pronounced Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone - Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.9(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0049 mM, comparison with inhibition of Klebsiella pneumoniae enzyme Go to the Ligand Summary Page
Results 1 - 10 of 83 > >>
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