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Deletion of the Gly600 Residue of Alicyclobacillus acidocaldarius Squalene Cyclase Alters the Substrate Specificity into that of the Eukaryotic‐Type Cyclase Specific to (3 S )‐2,3‐Oxidosqualene
Author(s) -
Hoshino Tsutomu,
Shimizu Kunio,
Sato Tsutomu
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200461523
Subject(s) - cyclase , residue (chemistry) , squalene , mutant , chemistry , biochemistry , enzyme , wild type , stereochemistry , gene
Removal service : A deletion mutant lacking the Gly600 residue of a prokaryotic squalene–hopene cyclase was prepared. Surprisingly, the mutant cyclase has no enzyme activity for 1 and 3 , but shows a high conversion ratio for 2 (see scheme). Deleting Gly600 alters the specificity from prokaryotic into that of eukaryotic‐type cyclases.