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Bicyclic triterpenes as new main products of squalene–hopene cyclase by mutation at conserved tyrosine residues
Author(s) -
Füll Christine
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03153-2
Subject(s) - squalene , mutant , cyclase , biochemistry , stereochemistry , amino acid , bicyclic molecule , aromatic amino acids , chemistry , tyrosine , catalysis , enzyme , gene
The catalytic cavity of the Alicyclobacillus acidocaldarius squalene–hopene cyclase is predominantly lined by aromatic amino acids. In mutant cyclases, the four tyrosine residues in the catalytic cavity were replaced by different amino acids. The mutants showed significant differences in catalytic behavior compared to the wild‐type and to each other. Mutants Y609L, Y609C and Y609S produced the bicyclic main product γ‐polypodatetraene, while Y495L and Y612L showed a wild‐type product pattern and produced hopene as the main product. Altered product patterns were also found with Y420 mutations.