It is of rising interest to expand an enzyme’s reaction portfolio beyond its physiological scope. In this endeavor, two challenges are of particular interest: Detailed understanding of the enzyme’s structure-function relationship as well as profound comprehension of the catalyzed chemical reaction pathways. Prerequisite in this task is the identification and variation of catalytic core elements, e.g. access, orientation and anchoring of a substrate via electronic interaction in tunnels or active site. In this paper we focused our engineering efforts on molecular anchors and highlighted the ability of hydrogen-bond mediated direction of cationic cascades in terpene cyclases. As a result, the engineered cyclase provides efficient access to value-added apocarotenoids by cutting down synthetic routes to a single step with unprecedented selectivity and high yields.
Angew. Chem. Int. Ed. 2021, 60
Als Highlight in Nature Catalysis besprochen:
Völler, JS. Directed cationic cascades Nat. Catal. 4, 262 (2021)
Weitere Informationen erhalten Sie von:
Prof. Bernhard Hauer
Institut Biochemie und Technische Biochemie,
Abteilung Technische Biochemie