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Lysine biosynthesis in penicillium chrysogenum regulation by general amino acid control and absence of lysine repression

Jaklitsch, W.M.; Roehr, M.; Kubicek, C.P.

Experimental Mycology 11(2): 141-149

1987


ISSN/ISBN: 0147-5975
DOI: 10.1016/0147-5975(87)90047-8
Accession: 005840121

Three strains of Penicillium chrysogenum (Q176, D6/1014/A, and P2), which display different rates of penicillin biosynthesis, were examined with respect to regulation of lysine biosynthetic enzymes at the level of their biosynthesis (i.e., homocitrate synthase, .alpha.-aminoadipate aminotransferase, .alpha.-aminoadipate reductase, saccharopine reductase, and saccharopine dehydrogenase). None of these enzymes became repressed to any extent when lysine was added to the culture medium. The same behavior was seen with all three strains. General amino acid control-evoked by histidine depletion (exogenous addition of amitrole)-caused derepression of saccharopine reductase and saccharopine dehydrogenase in strain Q176, whereas the other enzymes remained unaffected. In strains D6/1014/A and P2, the same behavior was seen with the exception of .alpha.-aminoadipate reductase, which was strongly derepressed in strain D6/1014/A and (to a lesser extent) in P2. Homocitrate synthase was not regulated by carbon catabolite repression in any of the strains.

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