Purification and characterization of epsilon-N-trimethyllysine L-amino oxidase from Neurospora crassa.
epsilon-N-Trimethyllysine L-amino oxidase from Neurospora crassa has been purified to electrophoretic homogeneity. A 1500-fold purification was obtained by centrifugation and successive column chromatography on ion-exchange and gel filtration supports. The enzyme has an estimated molecular weight of 160 000. It transforms epsilon-N-trimethyllysine into alpha-keto, epsilon-N-trimethylhexanoic acid by oxidative deamination. Kinetic studies of this new enzyme are reported and its probable physiological role is discussed.
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives; D008970:Molecular Weight; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D000594:Amino Acid Oxidoreductases; C023189:epsilon-N-trimethyllysine L-amino oxidase; D008239:Lysine