Deletion of the Gly600 Residue ofAlicyclobacillus acidocaldarius Squalene Cyclase Alters the Substrate Specificity into that of the Eukaryotic-Type Cyclase Specific to (3S)-2,3-Oxidosqualene-Reference-Cited by-同舟云学术

Deletion of the Gly600 Residue ofAlicyclobacillus acidocaldarius Squalene Cyclase Alters the Substrate Specificity into that of the Eukaryotic-Type Cyclase Specific to (3S)-2,3-Oxidosqualene

Published:2004-12-10 Issue:48 Volume:43 Page:6700-6703
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Hoshino Tsutomu,Shimizu Kunio,Sato Tsutomu

Publisher

Wiley

Subject

General Chemistry,Catalysis

Reference32 articles.

1. Squalene–hopene cyclase: catalytic mechanism and substrate recognition

2. Mechanismen der enzymatischen Bildung polycyclischer Triterpene

3. Enzyme Mechanisms for Polycyclic Triterpene Formation

4. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes

5. 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

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