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. 2019 Jul 23;12:186. doi: 10.1186/s13068-019-1524-6

Table 5.

Kinetic parameters of enzymes Tt_Hbd and St_Ter and their variants, purified from E. coli

Enzyme	NADH		NADPH
Enzyme	K_m (mM)	V_max (µmol/min/mg)	K_m (mM)	V_max (µmol/min/mg)
Hbd^a	0.05 ± 0.02^c	61.4 ± 7.2	1.1 ± 0.2^a	15.2 ± 2.5
Hbd (D31A)	0.06 ± 0.02	38.5 ± 4.5	0.03 ± 0.01	485.3 ± 34.2
Hbd (I32R)	0.08 ± 0.02	25.1 ± 6.3	0.04 ± 0.02	152.1 ± 12.2
Hbd (P36I)	0.08 ± 0.01	24.2 ± 2.1	0.04 ± 0.01	128.2 ± 15.3
Hbd M3 (D31A I32R P36I)	0.11 ± 0.02	26.6 ± 3.7	0.03 ± 0.01	764.9 ± 35.7
Ter^b	0.03 ± 0.01	18.2 ± 2.3	0.4 ± 0.1	12.2 ± 1.5
Ter M (E75A)	0.6 ± 0.1	10.3 ± 1.5	0.02 ± 0.01	68.1 ± 6.5

^aAcetoacetyl-CoA was substrate of Hbd assay

^bCrotonyl-CoA was the substrate of Ter assay

^cError represents one standard deviation, n = 3