
Lysine biosynthesis in Penicillium chrysogenum is regulated by feedback inhibition of α‐aminoadipate reductase
Author(s) -
Affenzeller K.,
Jaklitsch W.M.,
Hönlinger C.,
Kubicek C.P.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03062.x
Subject(s) - penicillium chrysogenum , biosynthesis , biochemistry , lysine , reductase , chemistry , enzyme , biology , amino acid
A partially purified preparation of α‐aminoadipate reductase (EC 1.2.1.31) from Penicillium chrysogenum is competitively inhibited by lysine ( K i or 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‐ 14 C)‐ α‐aminoadipate into protein‐bound lysine to a fifth. The distribution of radioactivity in the pathway metabolites α‐aminoadipate, saccharopine and lysine was consistent with the assumption of a lysine sensitive enzyme step in vivo between α‐aminoadipate and saccharopine. Hence lysine inhibition of α‐aminoadipate reductase may be of physiologic importance.