Published January 5, 2006
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Journal Article
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Stereoselective Incorporation of an Unsaturated Isoleucine Analogue into a Protein Expressed in E. coli
Abstract
The unsaturated amino acid 2-amino-3-methyl-4-pentenoic acid (E-Ile) was prepared in the form of its (2S,3S),(2R,3R) and (2S,3R),(2R,3S) stereoisomeric pairs. The translational activities of SS-E-He and SR-E-Ile were assessed in an E. coli strain rendered auxotrophic for isoleucine. SS-E-Ile was incorporated into the test protein mouse dihydrofolate reductase (mDHFR) in place of isoleucine at a rate of up to 72%; SR-E-Ile yielded no conclusive evidence for incorporation. ATP/PPi exchange assays indicated that SS-E-Ile was activated by the isoleucyl-tRNA synthetase at a rate comparable to that characteristic of isoleucine; SR-E-Ile was activated approximately 100-times more slowly than SS-E-Ile.
Additional Information
c2006 Wiley-VCH Verlag. Issue published online: 5 JAN 2006. Article first published online: 5 JAN 2006. Manuscript Received: 13 MAY 2005. This work was supported by NSF grant DMR0110437, by the Department of Defense through a NDSEG graduate fellowship to M.L.M., and by NATO through sabbatical support for T.M. The authors thank Kristi Kiick, Scott Ross, and Takuya Sakaki for their advice and assistance.Attached Files
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Additional details
- Eprint ID
- 53691
- DOI
- 10.1002/cbic.200500201
- Resolver ID
- CaltechAUTHORS:20150114-100618078
- DMR0110437
- NSF
- National Defense Science and Engineering Graduate (NDSEG) Fellowship
- NATO
- Created
-
2015-01-14Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field