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| Content Provider | Springer Nature Link |
|---|---|
| Author | Hijarrubia, M. Aparicio, J. Martín, J. |
| Copyright Year | 2002 |
| Abstract | α-Aminoadipate reductase (α-AAR) is a key enzyme in the branched pathway for lysine and β-lactam biosynthesis of filamentous fungi since it competes with α-aminoadipyl-cysteinyl-valine synthetase for their common substrate L-α-aminoadipic acid. The α-AAR activity in two penicillin-producing Penicillium chrysogenum strains and two cephalosporin-producing Acremonium chrysogenum strains has been studied. The α-AAR activity peaked during the growth-phase preceding the onset of antibiotic production, which coincides with a decrease in α-AAR activity, and was lower in high penicillin- or cephalosporin-producing strains. The α-AAR required NADPH for enzyme activity and could not use NADH as electron donor for reduction of the α-aminoadipate substrate. The α-AAR protein of P. chrysogenum was detected by Western blotting using anti-α-AAR antibodies. The mechanism of lysine feedback regulation in these two filamentous fungi involves inhibition of the α-AAR activity but not repression of its synthesis by lysine. This is different from the situation in yeasts where lysine feedback inhibits and represses α-AAR. Nitrate has a strong negative effect on α-AAR formation as shown by immunoblotting studies of α-AAR. The nitrate effect was reversed by lysine. |
| Starting Page | 270 |
| Ending Page | 277 |
| Page Count | 8 |
| File Format | |
| ISSN | 01757598 |
| Journal | Applied Microbiology and Biotechnology |
| Volume Number | 59 |
| Issue Number | 2-3 |
| e-ISSN | 14320614 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2002-05-08 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | Subscribed |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Applied Microbiology and Biotechnology Biotechnology |
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