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| Content Provider | Springer Nature Link |
|---|---|
| Author | Molog, Grietje Empt, Ursula Kuhlmann, Stephan van Uden, Wim Pras, Niesko Alfermann, August Petersen, Maike |
| Copyright Year | 2001 |
| Abstract | Cell-suspension cultures of Linum flavum L. (Linaceae) synthesize and accumulate aryltetrahydronaphthalene lignans with 6-methoxypodophyllotoxin as the main component. The experimental data indicate that the biosynthesis of 6-methoxypodophyllotoxin occurs via deoxypodophyllotoxin, β-peltatin, and β-peltatin-A methyl ether. The enzyme catalyzing the introduction of the hydroxyl group in position 6 is deoxypodophyllotoxin 6-hydroxylase (DOP6H). The enzyme was shown to be a cytochrome P450-dependent monooxygenase by blue-light reversion of carbon monoxide inhibition and inhibition by cytochrome c. DOP6H is a membrane-bound microsomal enzyme with a pH optimum of 7.6 and a temperature optimum of 26 °C. Deoxypodophyllotoxin is specifically accepted with an apparent K m of 20 µM and a saturation concentration of 200 µM; 4′-demethyldeoxypodophyllotoxin is the only other tested substrate accepted for hydroxylation. DOP6H predominantly accepts NADPH as electron donor; NADH can only sustain low hydroxylation activities. A synergistic effect of NADPH and NADH is not observed. The enzyme is saturated around 250 µM NADPH; the apparent K m for this substrate is 36 µM. |
| Starting Page | 288 |
| Ending Page | 294 |
| Page Count | 7 |
| File Format | |
| ISSN | 00320935 |
| Journal | Planta |
| Volume Number | 214 |
| Issue Number | 2 |
| e-ISSN | 14322048 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2001-07-21 |
| Publisher Place | Berlin/Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Plant Science |
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