Abstract
To provide insights into the structure-function relationships of oxidosqualene-lanosterol cyclase (ERG7) from Saccharomyces cerevisiae, the Phe699 was exchanged against hydrophilic polar uncharged residues Ser, Thr, Cys, Gln, and Tyr to characterize its product profile and functional role in ERG7 activity. Among the substitutions, only the ERG7(F699T) mutant produced novel protosta-13(17),24-dien-3beta-ol as the sole truncated rearrangement product. The results suggest that Phe699Thr mutation is likely to affect the C-17 cation stabilization during the rearrangement process.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Substitution*
-
Amino Acids / genetics
-
Crystallography, X-Ray
-
Intramolecular Transferases* / chemistry
-
Intramolecular Transferases* / genetics
-
Intramolecular Transferases* / metabolism
-
Models, Molecular
-
Mutation
-
Phenylalanine / chemistry
-
Phenylalanine / genetics
-
Protein Conformation
-
Saccharomyces cerevisiae / enzymology*
-
Saccharomyces cerevisiae / genetics*
-
Structure-Activity Relationship
-
Threonine / chemistry
-
Threonine / genetics
-
Triterpenes / chemistry
-
Triterpenes / isolation & purification*
Substances
-
Amino Acids
-
Triterpenes
-
protosta-13(17),24-dien-3beta-ol
-
Threonine
-
Phenylalanine
-
Intramolecular Transferases
-
lanosterol synthase