title: Charcterization and physiological function of a soluble L-amino acid oxidase in Corynebacterium.
abstract: A general L-amino acid oxidase (L-amino acid: oxygen oxidoreductase (deaminating), EC(1.4.3.2) has been characterized in Corynebacterium. The enzyme is soluble (MW 130000-140000) and is active with most L-alpha-amino acids but not with aspartate, threonine, proline and glycine. It is subject to substrate inhibition. This amino acid oxidase is induced along with catalase by growth in the presence of amino acids as a nitrogen source and is repressed when ammonium ions are present in the medium. Its probable physiological function is to allow the utilization of amino acids as a nitrogen source.
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification* / Q000502:physiology; D001224:Aspartic Acid; D002374:Catalase; D003352:Corynebacterium / Q000201:enzymology* / Q000254:growth & development; D003470:Culture Media; D004790:Enzyme Induction; D005998:Glycine; D009584:Nitrogen; D011392:Proline; D012995:Solubility; D013912:Threonine
chemical_list: D003470:Culture Media; D013912:Threonine; D001224:Aspartic Acid; D011392:Proline; D002374:Catalase; D000594:Amino Acid Oxidoreductases; D009584:Nitrogen; D005998:Glycine