Alpha-hydroxyglutarate oxidoreductase of Pseudomonas putida.
Oxidation of d-alpha-hydroxyglutarate to alpha-ketoglutarate is catalyzed by d-alpha-hydroxyglutarate oxidoreductase, an inducible membrane-bound enzyme of the electron transport particle [ETP; a comminuted cytoplasmic membrane preparation with enzymic properties and chemical composition resembling beef heart mitochondrial ETP (1)] of Pseudomonas putida P2 (P2-ETP). Treatment of P2-ETP with a nonionic detergent yields a preparation with the sedimentation characteristics of a soluble enzyme, but which retains an intact electron transport chain. Oxygen acts solely as a terminal electron acceptor and may be replaced by ferricyanide, 2,6-dichlorophenol indophenol, or mammalian cytochrome c. The oxidoreductase is specific for the d-isomer (K(m) = 4.0 x 10(-4)m for dl-alpha-hydroxyglutarate) and is distinct both from l- and d-malate dehydrogenases. Spectral studies suggest that the carrier sequence is substrate --> flavine or nonheme iron --> cyt b --> [cyt c] --> oxygen.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D002498:Centrifugation; D003470:Culture Media; D004579:Electron Transport; D005971:Glutamates / Q000378:metabolism; D005977:Glutarates / Q000378:metabolism*; D007656:Ketoglutaric Acids / Q000096:biosynthesis; D008239:Lysine / Q000378:metabolism; D008722:Methods; D011549:Pseudomonas / Q000201:enzymology*; D014465:Ultrasonics
D003470:Culture Media; D005971:Glutamates; D005977:Glutarates; D007656:Ketoglutaric Acids; D000429:Alcohol Oxidoreductases; D008239:Lysine