Amanote Research
Register
Sign In
Tryptophan 232 Within Oxidosqualene-Lanosterol Cyclase From Saccharomyces Cerevisiae Influences Rearrangement and Deprotonation but Not Cyclization Reactions
doi 10.1021/ol053134w.s001
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Site-Saturated Mutagenesis of Histidine 234 of Saccharomyces Cerevisiae Oxidosqualene-Lanosterol Cyclase Demonstrates Dual Functions in Cyclization and Rearrangement Reactions
Fatty Acylation Is Important but Not Essential for Saccharomyces Cerevisiae RAS Function.
Molecular and Cellular Biology
Cell Biology
Molecular Biology
A Manganese-Dependent Adenyl Cyclase in Baker's Yeast, Saccharomyces Cerevisiae.
Acta Chemica Scandinavica
Steroid Biosynthesis. Relative Efficiencies of Enzymic Transformation of Terminally Modified Squalene 2,3-Oxide Analogs Into Lanosterol Analogs by 2,3-Oxidosqualene Cyclase
Chemistry Letters
Chemistry
Tryptophan Permease Gene TAT2 Confers High-Pressure Growth in Saccharomyces Cerevisiae
Molecular and Cellular Biology
Cell Biology
Molecular Biology
Mutational Mapping of RAS-responsive Domains of the Saccharomyces Cerevisiae Adenylyl Cyclase.
Molecular and Cellular Biology
Cell Biology
Molecular Biology
Bipolar Orientation of Chromosomes in Saccharomyces Cerevisiae Is Monitored by Mad1 and Mad2, but Not by Mad3
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
Robust Orthogonal Recombination System for Versatile Genomic Elements Rearrangement in Yeast Saccharomyces Cerevisiae
Scientific Reports
Multidisciplinary
Tris(pentafluoroethyl)germane: Deprotonation and Hydrogermylation Reactions
Chemistry - A European Journal
Organic Chemistry
Catalysis
Chemistry
