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Site-Directed Mutagenesis of Putative Active-Site Residues in Squalene-Hopene Cyclase

✍ Scribed by Corinna Feil; Roderich Süssmuth; Günther Jung; Karl Poralla


Book ID
115131824
Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
553 KB
Volume
242
Category
Article
ISSN
1432-1327

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Altered product pattern of a squalene-ho
✍ Thorsten Merkofer; Catherine Pale-Grosdemange; Karl Ulrich Wendt; Michel Rohmer; 📂 Article 📅 1999 🏛 Elsevier Science 🌐 French ⚖ 177 KB

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 Phe6