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. Author manuscript; available in PMC: 2018 Feb 15.
Published in final edited form as: J Am Chem Soc. 2017 Feb 3;139(6):2351–2358. doi: 10.1021/jacs.6b11737

Table 1.

Biochemical analyses of orthogonal enzyme-substrate pairs.

Enzyme % WT light emissiona Normalized kcat/KMb λmax (nm) Compound
A 1.2 ± 0.35 0.041±0.016 612 graphic file with name nihms859494t1.jpg
D-luc
B 0.92 ±0.17 0.013 ± 0.004 616
C 94 ± 8.4 5.22 ± 0.58 570
A 0.19±0.02 0.034 ± 0.008 614 graphic file with name nihms859494t2.jpg
2b
B 0.33 ± 0.09 0.050 ± 0.020 614
C 17 ±5.2 5.0 ±1.3 574
A 0.16 ±0.02 0.253 ±0.065 614 graphic file with name nihms859494t3.jpg
2c
B 3.7 ± 0.76 1.09 ± 0.36 618
C 16 ± 2.3 8.2 ±2.2 600
A 0.47 ±0.01 0.121 ±0.025 _c graphic file with name nihms859494t4.jpg
2d
B 0.81 ± 0.09 0.155 ±0.061 604
C 22 ±2.3 6.0 ±1.7 570
A 38 ±13 17.1 ± 6.4 622 graphic file with name nihms859494t5.jpg
3b
B 200 ± 41 83 ±37 628
C 13 ± 2 13.1 ± 5.7 626
a

Values normalized to each compound’s corresponding emission with WT Fluc. Errors represent standard error of the mean for n = 3 measurements.

b

Kinetic constants are apparent values, determined via measurements of initial rates of light emission over a range of 2 μM to 10 mM. Errors represent standard error of the mean for n≥3 measurements. kcat values are relative to each compound’s corresponding value with WT Fluc. Errors represent standard error of the mean for n ≥ 3 measurements.

c

λmax value could not be determined due to low level of light emission.