Lysine biosynthesis in Penicillium chrysogenum is regulated by feedback inhibition of alpha-aminoadipate reductase.
A partially purified preparation of alpha-aminoadipate reductase (EC 1.2.1.31) from Penicillium chrysogenum is competitively inhibited by lysine (Ki of 0.26 mM). Exogenous addition of 10 mM L-lysine to resting mycelia of P. chrysogenum increased the intracellular lysine pool concentration 2-fold, but decreased the incorporation of (6-14C)-alpha-aminoadipate into protein-bound lysine to a fifth. The distribution of radioactivity in the pathway metabolites alpha-aminoadipate, saccharopine and lysine was consistent with the assumption of a lysine sensitive enzyme step in vivo between alpha-aminoadipate and saccharopine. Hence lysine inhibition of alpha-aminoadipate reductase may be of physiologic importance.
Affenzeller
K
K
Department of Microbial Biochemistry, Vienna Technical University, Austria.
Jaklitsch
W M
WM
Hönlinger
C
C
Kubicek
C P
CP
D015074:2-Aminoadipic Acid / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors*; D005246:Feedback; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine / Q000096:biosynthesis* / Q000494:pharmacology; D010407:Penicillium / Q000378:metabolism*; D010408:Penicillium chrysogenum / Q000187:drug effects / Q000378:metabolism*
D015074:2-Aminoadipic Acid; D000445:Aldehyde Oxidoreductases; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine