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. 2010 Sep 30;285(49):38270–38282. doi: 10.1074/jbc.M110.164293

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 5. — Steady-state analysis of cholest-4-en-3-one turnover by CYP142. A CYP142 cholest-4-en-3-one-oxidizing system was reconstituted using the spinach ferredoxin reductase/ferredoxin proteins and NADPH, as described under “Experimental Procedures.” The system was effective in driving 27-hydroxylation of both cholest-4-en-3-one and cholesterol, and data for substrate-dependent NADPH oxidation versus cholest-4-en-3-one concentration were fitted using the Michaelis-Menten equation to provide parameters of k_cat = 0.0062 ± 0.0004 min⁻¹ and K_m = 3.2 ± 0.8 μm.