. Author manuscript; available in PMC: 2016 Jan 31.

Published in final edited form as: Biochim Biophys Acta. 2014 Dec 10;1854(2):146–155. doi: 10.1016/j.bbapap.2014.12.003

Table 2.

Steady-state kinetic parameters for the DGD wild-type and mutant enzymes.^a

	AIB			AC6C			AC5C			Pyruvate
	K_M	k_cat	k_cat/K_M	K_M	k_cat	k_cat/K_M	K_M	k_cat	k_cat/K_M	k_cat/K_M
	(mM)	(s⁻¹)	(M⁻¹ s⁻¹)	(mM)	(s⁻¹)	(M⁻¹ s⁻¹)	(mM)	(s⁻¹)	(M⁻¹ s⁻¹)	(M⁻¹ s⁻¹)
WT	2.5 (0.3)	10.2 (0.3)	4100	25.3 (1.8)	0.78 (0.02)	31	4.7 (1.2)	0.56 (0.04)	120	51,000
RIIc1	1.9 (0.3)	1.00 (0.03)	530	7.3 (0.9)	0.36 (0.02)	49	2.1 (0.4)	0.24 (0.01)	110	23,000
RIIIc1	2.4 (0.2)	2.59 (0.05)	1100	4.7 (0.3)	0.51 (0.01)	110	2.3 (0.4)	0.4 (0.02)	170	31,000
RIIIc3	2.7 (0.3)	2.6 (0.07)	1000	8.9 (1.0)	0.66 (0.03)	74				35,000
RIIIc6	2.1 (0.4)	0.67 (0.03)	320	6.6 (0.6)	0.25 (0.01)	38				13,000
RIIIc12	1.9 (0.2)	2.3 (0.05)	1200	8.2 (1.2)	0.88 (0.05)	110				41,000
RIVc15	2.8 (0.3)	3.6 (0.12)	1300	10.5 (0.9)	1.49 (0.05)	140	1.2 (0.1)	0.46 (0.01)	380	23,000

Standard errors are given in parentheses. Errors on k_cat/K_M for pyruvate are ~15%.