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Crystalline Mammalian l-Amino Acid Oxidase from Rat Kidney Mitochondria

From the ¹ From the Section of Endocrinology and Metabolism of the University of Pittsburgh, Department of Medicine, and the Medical Center and Shadyside Hospitals, Pittsburgh, Pennsylvania

l-Amino acid oxidase has been crystallized from extracts of rat kidney mitochondria. Purification involved sonic extraction, ammonium sulfate fractionation, chromatography on diethylaminoethyl cellulose, and gel filtration through Sephadex G-200. The enzyme revealed a single protein band on starch gel electrophoresis and exhibited a single homogeneous peak (s_{20, w}⁰ = 10.5 S) in an ultracentrifuge.

The enzyme is a flavoprotein in which the prosthetic group appears to be flavin mononucleotide. On the basis of the flavin mononucleotide content of the enzyme (0.92%) and its molecular weight (88,900 ± 1,100), it has been concluded that the enzyme contains 2 moles of flavin mononucleotide per mole.

The enzyme catalyzes the oxidation of many -aminomonocarboxylic and -hydroxy acids (l configuration) but has no action on optically inactive acids such as glycine and -hydroxyisobutyric acid. The turnover numbers for the oxidation of l-leucine and of l-lactic acid were 6.3 and 26 moles per min per mole of flavin mononucleotide conjugated with enzyme, respectively.

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