Details
| Original language | English |
|---|---|
| Pages (from-to) | 233-244 |
| Number of pages | 12 |
| Journal | Catalysis Science and Technology |
| Volume | 13 |
| Issue number | 1 |
| Publication status | Published - 24 Nov 2022 |
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.
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
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In: Catalysis Science and Technology, Vol. 13, No. 1, 24.11.2022, p. 233-244.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Rational reprogramming of the sesquiterpene synthase BcBOT2 yields new terpenes with presilphiperfolane skeleton
AU - Nikolaiczyk, Vanessa
AU - Irwan, Jenny
AU - Nguyen, Trang
AU - Fohrer, Jörg
AU - Elbers, Philipp
AU - Schrank, Paul
AU - Davari, Mehdi D.
AU - Kirschning, Andreas
N1 - Funding Information: We thank Dr. Gerald Dräger (Leibniz Universität Hannover, Hannover, Germany) for excellent support in the structural analysis of MS spectrometric data. MDD is supported through funds from IPB Halle.
PY - 2022/11/24
Y1 - 2022/11/24
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85143593963&partnerID=8YFLogxK
U2 - 10.1039/d2cy01617f
DO - 10.1039/d2cy01617f
M3 - Article
AN - SCOPUS:85143593963
VL - 13
SP - 233
EP - 244
JO - Catalysis Science and Technology
JF - Catalysis Science and Technology
SN - 2044-4753
IS - 1
ER -