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1.14.14.23: cholesterol 7alpha-monooxygenase

This is an abbreviated version!
For detailed information about cholesterol 7alpha-monooxygenase, go to the full flat file.

Word Map on EC 1.14.14.23

Reaction

cholesterol
+
[reduced NADPH-hemoprotein reductase]
 +
O2
=
7alpha-hydroxycholesterol
 +
[oxidized NADPH-hemoprotein reductase]
 +
H2O

Synonyms

7alpha-hydroxylase, bile acid-synthetic enzyme, C7alphaOH, cholesterol 7 alpha-hydroxylase, cholesterol 7-alpha hydroxylase, Cholesterol 7-alpha-hydroxylase, Cholesterol 7-alpha-monooxygenase, cholesterol 7a-hydroxylase, cholesterol 7alpha hydroxylase, cholesterol 7alpha-hydroxylase, cholesterol-NADPH oxidoreductase, 7alpha-hydroxylating, CYP125A4, CYP7A, CYP7A1, Cyp7alpha1, CYPVII, cytochrome P450 125A4, EC 1.14.13.17, hepatic cholesterol 7alpha-hydroxylase, More, oxygenase, cholesterol 7alpha-mono-

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
                1.14.14.23 cholesterol 7alpha-monooxygenase

Engineering

Engineering on EC 1.14.14.23 - cholesterol 7alpha-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A204C
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene, the genetic variant shows less total cholesterol level decrease in response to dietary changes in different types of dietary intervention studies compared to C204 homozygotes, overview
A278C
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene
C16A
-
strongly decreased activity
C175A
-
decreased activity
C17A
-
increased activity
C444A
-
no activity
C44A
-
decreased activity
C476A
-
no activity
C554T
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene
C69A
-
no effect on activity
C90A
-
decreased activity
T104L
the mutant is similar to the wild-type in ligand binding and catalytic properties and readily crystallizes with substrates. The structure of the T104L mutant in complex with cholest-4-en-3-one explicitly identifies key residues involved in 7alpha-hydroxylation
additional information