User:Martha Blakely/Sandbox 1: Difference between revisions
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[[Image:FAD.jpg]] Flavin moiety of FAD cofactor with an empty N5 bond. | [[Image:FAD.jpg]] Flavin moiety of FAD cofactor with an empty N5 bond. | ||
Each monomer has its own <scene name='User:Martha_Blakely/Sandbox_1/ | Each monomer has its own <scene name='User:Martha_Blakely/Sandbox_1/Fad_cofactors2/1'>FAD cofactor</scene> covalently bound. The FAD molecule is situated on the opposite end of the active site away from the entrance into the cavity. It aids in binding substrates and inhibitors which seem to be situated between Tyr398 and Tyr435 when bonded to the N5 position of the FAD cofactor (generally called “flavin moiety”). Inhibitors and substrates must maneuver past these tyrosine residues, which contain phenol side chains, in order to bond to the N5 position of the FAD cofactor. These three together, the flavin, Tyr398, and Tyr435, form an aromatic cage. | ||
The implications of these residues are important to know for their own effects on substrate binding. These important residues also show that further knowledge of the three-dimensional structure of MAO-B is important in the development of enzyme inhibitors. | The implications of these residues are important to know for their own effects on substrate binding. These important residues also show that further knowledge of the three-dimensional structure of MAO-B is important in the development of enzyme inhibitors. | ||
