TY - JOUR A1 - Awakawa, Takayoshi A1 - Abe, Ikuro T1 - Molecular basis for the plasticity of aromatic prenyltransferases in hapalindole biosynthesis JF - Beilstein Journal of Organic Chemistry PY - 2019/// VL - 15 SP - 1545 EP - 1551 SN - 1860-5397 DO - 10.3762/bjoc.15.157 PB - Beilstein-Institut JA - Beilstein J. Org. Chem. UR - https://doi.org/10.3762/bjoc.15.157 KW - crystal structure KW - cyanobacteria KW - Friedel–Crafts reaction KW - hapalindole KW - prenyltransferase N2 - Aromatic prenyltransferases (PTases) are enzymes that catalyze Friedel–Crafts reactions between aromatic compounds and isoprenoid diphosphates. In hapalindole biosynthesis, the aromatic PTases AmbP1 and AmbP3 exhibit surprisingly plastic selectivities. AmbP1 not only transfers the geranyl group on the C-3 of cis-indolylvinyl isonitrile, but also on the C-2, which is supressed in the presence of Mg2+ ions. AmbP3 transfers the dimethylallyl group on C-2 of hapalindole U in the reverse manner, but on C-2 of its C-10 stereoisomer in the normal manner. This review highlights the molecular bases of the AmbP1 and AmbP3 functions, elucidated through their X-ray crystal structures. The knowledge presented here will contribute to the understanding of aromatic PTase reactions and will enhance their uses as biocatalysts. ER -