Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase

Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase

Escherichia coli lipoic acid ligase (LplA) catalyzes ATP-dependent covalent ligation of lipoic acid onto specific lysine side chains of three acceptor proteins involved in oxidative metabolism. Our lab has shown that LplA and engineered mutants can ligate useful small-molecule probes such as alkyl a...

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Bibliographic Details
Main Authors: Puthenveetil, Sujiet, Liu, Daniel S., White, Katharine Alice, Thompson, Samuel M., Ting, Alice Y.
Other Authors: Massachusetts Institute of Technology. Department of Chemistry
Format: Article
Language:en_US
Published: American Chemical Society 2012
Online Access:http://hdl.handle.net/1721.1/69549
https://orcid.org/0000-0002-8277-5226

Internet

http://hdl.handle.net/1721.1/69549
https://orcid.org/0000-0002-8277-5226

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