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. Author manuscript; available in PMC: 2019 Mar 1.
Published in final edited form as: J Inorg Biochem. 2018 Jan 12;180:235–245. doi: 10.1016/j.jinorgbio.2018.01.010

Table 4.

Kinetic constants for 26-hydroxylation of cholesterol and cholest-4-en-3-one by purified CYP124A1, CYP125A1, and CYP142A1. KD is the spectroscopically determined binding constant.

Substrate Enzyme KD (nM) Kmapp (μM) kcatapp (min−1) kcatapp/Kmapp (μM−1 min−1)
Cholesterol 124A1 - 11.6 1.5 0.13
125A1 107 10.7 28 2.6
142A1 18.4 7.7 16.7 2.2

Cholest-4-en-3-one 124A1 1056 20.8 11.7 0.56
125A1 1180 20.8 175 8.4
142A1 114 11.8 84 7.1