in contrast to M602K and wild-type enzyme, the quinone in D298K does not react with any of the hydrazines. D298K shows no activity toward oxidative deamination of 2-phenylethylamine. The quinone formed in D298K is trapped in a conformation that can not react with amines. D298K contains a quinone other than topaquinone
mutation has moderate effects on the kinetics of catalysis (2.7fold and 8fold decrease in kcat using ethylamine and benzylamine as substrates), the same mutation slows cofactor formation by about 45-fold relative to that of the wild-type enzyme. The Y305A mutant forms at least two species: primarily topaquinone at lower pH and a species with a blue-shifted absorbance at high pH
gain-of-function mutant MAO-N-D3, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site
genetic variant MOA-N-3 exhibits improved activity towards a range of amine substrates compared to the wild-type enzyme, including chiral secondary amines
gain-of-function mutant MAO-N-D5 is able to oxidise tertiary amines, structure analysis, overview. Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site. The two additional mutations, Thr384Asn and Asp385Ser, appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382, again altering the steric and electronic character of the active site near FAD
the mutant of AOC3 changes substrate preferences toward those of copper-containing monoamine oxidase AOC2 with high activity towards 2-phenylethylamine
construction of AOC3-KO mice which show white adipose tissue with lower CD45 mRNA levels and fewer CD45+ leukocytes and diminished infiltration by T cells, macrophages, natural killer, and natural killer T cells, the phenotype is not rescued by human SSAO/VAP-1 expression on adipocytes under the control of aP2, overview