Biochemical and Biophysical Research Communications
Regular ArticleDramatic Species Differences in the Susceptibility of Monoamine Oxidase B to a Group of Powerful Inhibitors
References (0)
Cited by (53)
Privileged scaffolds as MAO inhibitors: Retrospect and prospects
2018, European Journal of Medicinal ChemistryCitation Excerpt :Structure and inhibitor binding experiments displayed that the obstruction in conformation flexibility of MAO-B inhibitors is due to bulky Phe side chain which reduces the space of the entrance cavity [53]. This was considered as the structural rationale for discrepancy in binding affinities of bovine and human MAO-B preparations [54] and warn the researchers towards potential dangers of using different MAO sources for development of human MAO inhibitors [55]. Another difference between active site cavity structures is the presence of Tyr326 side chain in MAO-B. Although, there it dit not directly partition the two cavities but produced a less pronounced restriction in hMAO-A where Ile335 occupies that position.
Monoamine oxidase inhibitory activities of heterocyclic chalcones
2015, Bioorganic and Medicinal Chemistry Lettersα-Tetralone derivatives as inhibitors of monoamine oxidase
2014, Bioorganic and Medicinal Chemistry LettersInhibition of monoamine oxidase by 8-[(phenylethyl)sulfanyl]caffeine analogues
2012, Bioorganic and Medicinal ChemistryCitation Excerpt :The interaction of inhibitors via a potential tight-binding mechanism has been reported previously. For example, chromone carboxamides display a quasi-reversible binding to human MAO-B,34,35 while oxadiazolones are reported to bind reversibly and time-dependently to rat brain MAO-B.36 Mazouz and colleagues has also described a series of reversible and extremely tight-binding MAO-B specific inhibitors.37 The reversibility of MAO-B inhibition by compound 1b was further demonstrated by constructing a set of Lineweaver–Burk plots for the inhibition of MAO-B. For this purpose, the initial catalytic rates were measured in the presence of three different concentrations of 1b, and in the absence of inhibitor.
Kinetic behavior and reversible inhibition of monoamine oxidases-enzymes that many want dead
2011, International Review of NeurobiologyStructural properties of human monoamine oxidases A and B
2011, International Review of NeurobiologyCitation Excerpt :These cavities comprise the bipartite cavity structure of human MAO-B and are probably similar for MAO-B preparations from other sources such as rat or bovine. In this context, Ile199 is replaced by a Phe in the bovine enzyme which accounts for differences observed in its binding affinities with reversible inhibitors expected to traverse both substrate and entrance cavities (Hubálek et al., 2005; Krueger et al., 1995). To date, only one inhibitor, 2-benzofuranyl-imidazoline (Bonivento et al., 2010), has been shown to specifically bind to the entrance cavity with no evidence for any binding into the substrate cavity (Fig. 3).