Improving the production of 9α-hydroxy-4-androstene-3,17-dione from phytosterols by 3-ketosteroid-Δ1-dehydrogenase deletions and multiple genetic modifications in Mycobacterium fortuitum

Table 1 The KstD enzyme activity (mU/mg total soluble protoplast protein) of ATCC 35855

Substrate	KstD1		KstD2		KstD3		KstD4		KstD5
	Specific Activity^a	Rel. Activity^b	Specific Activity	Rel. Activity	Specific Activity	Rel. Activity	Specific Activity	Rel. Activity	Specific Activity	Rel. Activity
AD	2.92 ± 1.14	100	261.75 ± 4.51	100	60.61 ± 1.43	100	0.93 ± 0.14	100	0.95 ± 0.18	100
4-HP	3.43 ± 1.06	117.37	533.41 ± 2.60	203.78	51.78 ± 2.87	85.43	0.55 ± 0.14	59.93	0.83 ± 0.32	88.03
9-OHAD	3.17 ± 0.80	108.46	2104.38 ± 43.3	803.94	19.03 ± 1.43	31.41	0.29 ± 0	31.56	0.29 ± 0.49	30.89
9-OHHP	2.75 ± 0	94.09	1203.52 ± 43.3	459.78	13.77 ± 2.48	22.73	1.35 ± 0.25	145.15	1.16 ± 0.18	122.14

^aValues (shown as mean ± S.E.M., n = 3) simply indicate the relative performance on substrates using the identical KstD enzyme
^bThe activity of each KstD is initially evaluated using AD as the substrate. This is set at 100% to indicate the relative activity against other substrates. The inhibition effect of methanol and PMS on the KstD activity was ignored

ISSN: 1475-2859