. Author manuscript; available in PMC: 2013 Jan 18.

Published in final edited form as: J Am Chem Soc. 2012 Jan 5;134(2):792–795. doi: 10.1021/ja209325n

Table 1.

Ligation efficiencies of lipoic acid ligase variants with the three frans-cyclooctene substrates (TCO1-3). The relative abilities of wild-type and mutant ligases to ligate TCO1-3 onto LplA acceptor peptide (LAP) were measured by an HPLC assay after 30 min. reaction time. Average, normalized product percentages from triplicate measuremeasurements are shown. (--) indicates no detectable product. Errors, ± 1 s. d.

Ligase	Wi Id-type	Trp37→Gly	Trp37→lie	Trp37→Val
Probe	Wi Id-type	Trp37→Gly	Trp37→lie	Trp37→Val
TC01	0.5 ±0.0	--	0.5 ±0.4	--
TC02	2.6 ±0.9	52.6 ± 1.1	77.8 ± 1.6	100.0 ±8.3
TC03	6.5 ± 1.0	22.6 ± 2.0	6.0 ± 0.6	6.6 ± 0.6