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...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
American Chemical Society
2012
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| Online Access: | http://hdl.handle.net/1721.1/69549 https://orcid.org/0000-0002-8277-5226 |