Deamination of methylamine by semicarbazidesensitive amine oxidase in human umbilical artery and rat aorta
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2014, Archives of Biochemistry and BiophysicsCitation Excerpt :Recombinant AOC3s produced in HEK and S2 cells were expressed without the transmembrane domain (i.e. residues 29–763 were expressed). In addition to the currently known endogenous substrates for AOC3 (i.e. methylamine and aminoacetone [71,72]), rAOC3 oxidizes benzylamine in vitro, but does not oxidize the diamines histamine or putrescine, unlike rAOC1 (Table 1) [49,70]. The AOC3 monomer has six predicted N-linked and three putative O-linked glycosylation sites.
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2011, Journal of Biological ChemistryCitation Excerpt :The activation of human lung VAP-1 by human plasma is greater if the plasma originates from diabetic patients or following heart myocardial infarction (10). The physiological substrates for SSAOs are not clearly defined, but the soluble amines methylamine and/or aminoacetone could be among the naturally occurring substrates for SSAOs (11). The majority of studies with copper-dependent amine oxidases have been conducted with the nonphysiological substrate benzylamine, as enzymatic activity with this substrate can be monitored spectroscopically with ease.
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2006, Journal of Biological ChemistryCitation Excerpt :This is consistent with the tetrameric form of the native E. coli YeiG demonstrated using analytical gel filtration (121.2 kDa). Extensive dimer/dimer contacts contain comparable amounts of hydrophobic (5) and hydrophilic (6) residues. The 2 times smaller dimer/dimer contacts (seven residues) are more hydrophilic (Glu99, Ser101, Asp103, and Lys200).