Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17a, 35037 Marburg, Germany.
Org Lett. 2012 Sep 21;14(18):4882-5. doi: 10.1021/ol302207r. Epub 2012 Sep 7.
Prenyltransferases of the dimethylallyl-tryptophan synthase (DMATS) superfamily catalyze Friedel-Crafts alkylation with high flexibility for aromatic substrates, but the high specificity for dimethylallyl diphosphate (DMAPP) prohibits their application as biocatalysts. We demonstrate here that at least one methyl group in DMAPP can be deleted or shifted to the δ-position. For acceptance by some DMATS enzymes, however, a double bond must be situated at the β-position. Furthermore, the alkylation position of an analogue can differ from that of DMAPP.
二甲基烯丙基色氨酸合酶（DMATS）超家族的 prenyltransferases 可催化对芳香族底物具有高灵活性的 Friedel-Crafts 烷基化反应，但对二甲基烯丙基二磷酸（DMAPP）的高特异性阻止了它们作为生物催化剂的应用。在这里，我们证明 DMAPP 中的至少一个甲基可以被删除或转移到δ-位。然而，为了被一些 DMATS 酶接受，双键必须位于β-位。此外，类似物的烷基化位置可以与 DMAPP 的不同。
