z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here