Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537349 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2005 | 9 Pages |
Abstract
The open reading frame YNR064c in Saccharomyces cerevisiae encodes a protein tentatively assigned as similar to a bacterial dehalogenase. In this study we conclude that the YNR064c protein displays characteristics of an epoxide hydrolase belonging to the α/β-hydrolase fold family of enzymes. Endogenous expression of the protein in S. cerevisiae was confirmed and a His-tagged variant of the protein was heterologously expressed in both Escherichia coli and Pichia pastoris for isolation and characterization. The YNR064c protein displayed low but reproducible epoxide hydrolase activity with racemic phenanthrene 9,10-oxide and trans- or cis-stilbene oxide. Phylogenetic analysis of related gene products found in various microorganisms suggested that the YNR064c protein is a member of a new subclass of α/β-hydrolase fold enzymes.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Lisa T. Elfström, Mikael Widersten,