Semicarbazide-sensitive amine oxidase acts as a vascular-adhesion protein, mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions
synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes. Semicarbazide-sensitive amine oxidase is involved in the following biological processes: vision, inflammatory response, biogenic amine metabolism, catecholamine metabolism, amine metabolism, cell adhesion
the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
VAP-1/SSAOs convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases, MAOs, but their substrate specificities are partly overlapping
T0901317 inhibits SSAO gene expression and its activity in atherogenic apoE-/- mice. The atheroprotective effect of LXR agonist T0901317 is related to the inhibition of SSAO gene expression and its activity
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide
the catalytic mechanism can be divided into two half-reactions: a reductive half-reaction in which a primary amine substrate is oxidized to its corresponding aldehyde with the concomitant reduction of the organic cofactor 2,4,5-trihydroxyphenylalanine quinone and an oxidative half-reaction in which reduced 2,4,5-trihydroxyphenylalanine quinone is re-oxidized with the reduction of molecular oxygen to hydrogen peroxide