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1.14.14.25: cholesterol 24-hydroxylase

This is an abbreviated version!
For detailed information about cholesterol 24-hydroxylase, go to the full flat file.

Word Map on EC 1.14.14.25

Reaction

cholesterol
+
[reduced NADPH-hemoprotein reductase]
+
O2
=
(24S)-cholest-5-ene-3beta,24-diol
+
[oxidized NADPH-hemoprotein reductase]
+
H2O

Synonyms

24S-hydroxylase, CH24H, cholesterol 24-hydroxylase, cholesterol 24-monooxygenase, cholesterol 24S hydroxylase, cholesterol 24S-hydroxylase, cholesterol hydroxylase, cholesterol-24S-hydroxylase, CYP46, CYP46A, CYP46A1, cytochrome P-450 46A1, cytochrome P450 46A1, cytochrome P450 cholesterol 24-hydroxylase, EC 1.14.13.98

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.25 cholesterol 24-hydroxylase

Engineering

Engineering on EC 1.14.14.25 - cholesterol 24-hydroxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1309C
-
destroys its heme structure, resulting in the complete lack of cholesterol 24-hydroxylase activity
K422A
site-directed mutagenesis, the K422A mutant retains the ability to be activated by EFV, although to a slightly lower extent than wild-type CYP46A1. The cholesterol-bound K422A mutant also shows cooperativity similar to cholesterol-bound wild-type CYP46A1. Binding to NADPH cytochrome P450 oxidoreductase is reduced compared to the wild-type
K94A
site-directed mutagenesis, the K94A replacement produces inactive P420 protein
R138A
site-directed mutagenesis, binding to NADPH cytochrome P450 oxidoreductase is reduced compared to the wild-type
R139A
site-directed mutagenesis, binding to NADPH cytochrome P450 oxidoreductase is reduced compared to the wild-type
R147A
site-directed mutagenesis, binding to NADPH cytochrome P450 oxidoreductase is unaltered compared to the wild-type
R424A
site-directed mutagenesis, the R424A mutant shows a total loss of the ability to be activated by EFV. The R424A replacement affects EFV binding to the allosteric site and cholesterol binding to the CYP46A1 active site. Binding to NADPH cytochrome P450 oxidoreductase is reduced compared to the wild-type
additional information