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. Author manuscript; available in PMC: 2017 Sep 16.

Published in final edited form as: ACS Chem Biol. 2016 Aug 5;11(9):2642–2654. doi: 10.1021/acschembio.6b00479

Table 2.

K_d Values from Equilibrium Substrate Binding Assays^a

Substrate	Enzyme
Substrate	MycCI	MycCI-RhFRED	TylHI	TylHI-RhFRED	MycCI_S172A
3	40 ± 4	40 ± 2	N.B.^b	N.B.	63 ± 5
5	17 ± 1	15.0 ± 0.8	N.B.	N.B.	23 ± 3
8	19 ± 2	15 ± 2	N.B.	1524 ± 546	9.2 ± 1.0
9	0.001 ± 0.001	0.005 ± 0.001	1291 ± 59	1230 ± 134	0.003 ± 0.004
10	3.3 ± 0.3	3.0 ± 0.3	433 ± 40	469 ± 39	1.35 ± 0.09
11	0.006 ± 0.004	0.010 ± 0.003	275 ± 22	205 ± 20	0.04 ± 0.01
12	0.045 ± 0.006	0.038 ± 0.005	0.60 ± 0.03	0.66 ± 0.05	0.12 ± 0.04

^a

K_d values are in μM. Reported errors are those obtained from fitting data averaged from experiments performed at least in triplicate.

^b

N.B. = no binding detected.