Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

PubChem5831 (2S)-2-phenyloxirane

Synonyms: CCRIS 4093, AG-E-52543, CHEBI:45389, ANW-24218, AC1L3FTN, ...

Rink, R. et al., Latham, G.J. et al., Rui, L. et al., Gadberry, M.G. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CCRIS 4093

In all studies, (R)-styrene oxide caused greater toxicity than the (S) enantiomer, especially in the liver [1].

High impact information on CCRIS 4093

In contrast, the template containing R-styrene oxide at the second position of N-ras 61 was a very poor substrate for replication, a result which correlates well with the observed lethality of this lesion in vivo [2].
Pre-steady-state analysis of the conversion of (R)-styrene oxide by the Y215F and Y215A mutants showed that the 1000-fold elevated K(m) values were mainly caused by a 15-40-fold increase in K(S) and a 20-fold reduction in the rate of alkylation [3].
Computer modeling indicated that this mutation significantly alters (R)-styrene oxide binding in the active site [4].

References

Pneumotoxicity and hepatotoxicity of styrene and styrene oxide. Gadberry, M.G., DeNicola, D.B., Carlson, G.P. Journal of toxicology and environmental health. (1996) [Pubmed]
The replication fate of R- and S-styrene oxide adducts on adenine N6 is dependent on both the chirality of the lesion and the local sequence context. Latham, G.J., Zhou, L., Harris, C.M., Harris, T.M., Lloyd, R.S. J. Biol. Chem. (1993) [Pubmed]
Tyrosine residues serve as proton donor in the catalytic mechanism of epoxide hydrolase from Agrobacterium radiobacter. Rink, R., Kingma, J., Lutje Spelberg, J.H., Janssen, D.B. Biochemistry (2000) [Pubmed]
Protein engineering of epoxide hydrolase from Agrobacterium radiobacter AD1 for enhanced activity and enantioselective production of (R)-1-phenylethane-1,2-diol. Rui, L., Cao, L., Chen, W., Reardon, K.F., Wood, T.K. Appl. Environ. Microbiol. (2005) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

Editor

Share