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. Author manuscript; available in PMC: 2017 Aug 9.
Published in final edited form as: Biochemistry. 2016 Jul 29;55(31):4356–4365. doi: 10.1021/acs.biochem.6b00532

Figure 4.

Figure 4

Product formation rates (A), NADPH consumption rates (B), and coupling efficiencies (C) with various substrates for P450 17A1 mutations relative to wild-type enzyme, as well as b5 effects on coupling (D). Color code for each steroid matches text in Tables 2–4.