Squalene–hopene cyclase: insight into the role of the methyl group on the squalene backbone upon the polycyclization cascade. Enzymatic cyclization products of squalene analogs lacking a 26-methyl group and possessing a methyl group at C(7) or C(11)
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2004/OB/B404287E
Reference28 articles.
1. Squalene–hopene cyclase: catalytic mechanism and substrate recognition
2. Enzyme Mechanisms for Polycyclic Triterpene Formation
3. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes
4. Squalene–hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring
5. Site-directed Mutagenesis Experiments on the Putative Deprotonation Site of Squalene-hopene Cyclase fromAlicyclobacillus acidocaldarius
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