Role of L-lysine-alpha-ketoglutarate aminotransferase in catabolism of lysine as a nitrogen source for Rhodotorula glutinis.
Wild-type and saccharopine dehydrogenaseless mutant strains of Rhodotorula glutinis grew in minimal medium containing lysine as the sole nitrogen source and simultaneously accumulated, in the culture supernatant, large amounts of a product identified as alpha-aminoadipic-delta-semialdehyde. The saccharopine dehydrogenase and pipecolic acid oxidase levels remained unchanged in wild-type cells grown in the presence of ammonium or lysine as the nitrogen source. Lysine-alpha-ketoglutarate aminotransferase activity was demonstrated in ammonium-grown cells. This activity was depressed in cells grown in the presence of lysine as the sole source of nitrogen.
D051306:L-Lysine 6-Transaminase; D008239:Lysine / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology*; D009154:Mutation; D009584:Nitrogen / Q000378:metabolism*; D012248:Rhodotorula / Q000201:enzymology* / Q000254:growth & development; D012441:Saccharomyces cerevisiae / Q000254:growth & development; D000637:Transaminases / Q000235:genetics / Q000378:metabolism*
D000637:Transaminases; D051306:L-Lysine 6-Transaminase; D008239:Lysine; D009584:Nitrogen