. 2014 Mar;196(6):1275–1285. doi: 10.1128/JB.00026-14

TABLE 3.

Substrate specificities of the DmdB isozymes^a

Substrate	Relative activity (%)
Substrate	PU_DmdB1	RPO_DmdB1	RPO_DmdB2	RL_DmdB1	RL_DmdB2	PA_DmdB1	BTH_DmdB2
MMPA	100	100	100	100	100	100	100
Acetate	10	0.0^b	10	151	0.0^b	110	0.0^b
Propionate	13	77	16	126	72	124	45
Acrylate	50	79	56	6	29	65	15
Butyrate	160	36	73	81	113	121	93
Isobutyrate	13	30	12	10	7	48	5
Crotonate	2	109	63	32	41	63	87
Methylbutyrate	8	10	39	20	18	24	23
Valerate	18	31	51	49	179	91	68
Isovalerate	8	19	14	15	5	18	4
Hexanoate	5	17	27	17	62	12	94
Caprylate	0.0^b	0.0^b	0.0^b	0.0^b	0.0^b	0.0^b	1
Caprate	0.0^b	0.0^b	0.0^b	0.0^b	0.0^b	0.0^b	0.0^b

Relative activity values expressed as a percentage of the total specific activity as measured with MMPA (100%). All standard errors are from three independent experiments and are within 3%. Specific activities in units mg⁻¹ of protein (±SE) defined as 100% were as follows: PU_DmdB1, 28 ± 1; RPO_DmdB1, 15 ± 3; RPO_DmdB2, 17 ± 3; RL_DmdB1, 24 ± 2; RL_DmdB2, 16 ± 2; PA_DmdB1, 32 ± 2; and BTH_DmdB2, 25 ± 4.

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