@Article{IPB-267,
author = {Nikolaiczyk, V. and Irwan, J. and Nguyen, T. and Fohrer, J. and Elbers, P. and Schrank, P. and Davari, M. D. and Kirschning, A.},
title = {{Rational reprogramming of the sesquiterpene synthase BcBOT2 yields new terpenes with presilphiperfolane skeleton}},
year = {2023},
pages = {233-244},
journal = {Catal. Sci. Technol.},
doi = {10.1039/d2cy01617f},
url = {https://doi.org/10.1039/D2CY01617F},
volume = {13},
abstract = {Computer-aided rational design of the substrate binding pocket of sesquiterpene synthases BcBOT2 from Botrytis cinerea yielded FPP cyclization products with presilphiperfolane backbone other than the naturally formed sesquiterpene presilphiperfolan-8β-ol. Particularly, amino acids W118 and F138 were found to strongly control the stability and conformation of key cationic intermediates. The W118Q variant forms only presilphiperfolan-9β-ol, whereas the exchange of amino acids at position 138, such as F138V, has a fundamental effect on the course of the cationic cascade. Here, the 1,3-hydride shift en route to presilphiperfolan-8β-ol is suppressed and substituted by a so far unknown 1,2-hydride shift that leads to presilphiperfol-1-ene and presilphiperfolan-1α-ol along with β-caryophyllene and the so far unknown caryophyllene-8β-ol.}    
}