EC Number   |
|---|
    1.4.3.4 | - |
| 1.4.3.4 | crystal structures of human MAO B in complex with the three inhibitors (safinamide, 7-(3-chlorobenzyloxy)-4-(methylamino)methylcoumarin or 7-(3-chlorobenzyloxy)-4-carboxaldehydecoumarin) reveal that they all bind noncovalently to the enzyme |
| 1.4.3.4 | hanging drop vapour diffusion method, crystal structure of the enzyme complexed with the specific inhibitor, clorgyline, at 3.2 A resolution |
| 1.4.3.4 | hanging drop vapour-diffusion method at 277K with a reservoir containing 12% w/v polyethylene glycol 2000 monomethylether, 100 mM sodium acetate, 100 mM sodium phosphate buffer, pH 6.2, and 26% v/v glycerol. Enzyme complexed with clorgyline, 3.2 A resolution, crystals belong to the space group P4(3)2(1)2, with unit-cell parameters a = b = 158.2, c = 258.4 A |
| 1.4.3.4 | MAO A, X-ray diffraction structure determination at 3.3 A resolution. The dimer structure of rat MAO A is more readily crystallized than its monomeric form |
| 1.4.3.4 | MAO-A, X-ray diffraction structure determination at 2.2 A resolution. MAO-B in complex with a range of inhibitors, X-ray diffraction structure determination at 1.65 A resolution. The human MAO-A monomer species is more likely to crystallize than its dimeric form |
| 1.4.3.4 | sitting-drop vapor diffusion method, crystal structures of MAO B in complex with trans,trans-farnesol and that of the I199F MAO B mutant protein |
| 1.4.3.4 | sitting-drop vapor diffusion method, mutant enzymes Y435H, Y435F, Y435L, Y435W and wild-type enzyme in complex with p-nitrobenzylamine |
| 1.4.3.4 | sitting-drop vapour diffusion method,1.7 A structure of the reversible isatin-MAO-B complex, 2.3 A structure of the 1,4-diphenyl-2-butene-MAO-B complex, 2.2 A structure of the tranylcypromine-MAO B complex, 2.4 A structure of the N-(2-aminoethyl)-p-chlorobenzamide-MAO-B complex, 3.1 A structure of the lauryldimethylamine N-oxide-MAO-B complex |
| 1.4.3.4 | sitting-drop vapour diffusion method. Crystal structures of MAO B in complex with four of the N-propargylaminoindane class of MAO B inhibitors, rasagiline, N-propargyl-1(S)-aminoindane, 6-hydroxy-N-propargyl-1(R)-aminoindane, and N-methyl-N-propargyl-1(R)-aminoindane are determined at a resolution of better than 2.1 A. Rasagiline, 6-hydroxy-N-propargyl-1(R)-aminoindane, and N-methyl-N-propargyl-1(R)-aminoindane adopt essentially the same conformation with the extended propargyl chain covalently bound to the flavin and the indane ring located in the rear of the substrate cavity. N-propargyl-1(S)-aminoindane binds with the indane ring in a flipped conformation with respect to the other inhibitors, which causes a slight movement of the Tyr326 side chain |
