Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues

✍ Scribed by Thorsten Merkofer; Catherine Pale-Grosdemange; Karl Ulrich Wendt; Michel Rohmer; Karl Poralla

• Book ID: 104260943
• Publisher: Elsevier Science
• Year: 1999
• Tongue: French
• Weight: 177 KB
• Volume: 40
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(99)00145-8

✦ Synopsis

Amino acid residues lining the catalytic cavity of squalene-hopene cyclase of Alicyclobacillus acidocaldarius have been mutated. Alterations of His451 to Ala and Trp489 to Ala resulted in reduced enzymatic activity, while the product patterns were identical to that of the wild-type. Mutation of Phe601 to Ala led to the enhanced formation of a tetracyclic triterpene, 17-isodammara-20(21),24-diene 4, and of Tyr420 to Ala to a significant alteration of the product pattern.