title: Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase.
abstract: Benzylamine oxidase (EC 1.4.3.6) from the yeast Pichia pastoris is a 106 kDa quinoprotein containing one copper atom per molecule. It has a broad substrate specificity ranging from butylamine to peptidyl lysine in collagen and elastin. The kinetic data obtained using lysine-containing model peptides as substrates indicate an astonishing similarity to mammalian lysyloxidase. This similarity is further supported by the inhibition of both enzymes with beta-aminopropionitrile.
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D001595:Benzylamine Oxidase / Q000378:metabolism*; D007700:Kinetics; D008995:Monoamine Oxidase / Q000378:metabolism*; D010843:Pichia / Q000201:enzymology*; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D004718:Saccharomycetales / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000594:Amino Acid Oxidoreductases; D001595:Benzylamine Oxidase; D008249:Protein-Lysine 6-Oxidase; D008995:Monoamine Oxidase