1.14.15.15: cholestanetriol 26-monooxygenase

This is an abbreviated version!
For detailed information about cholestanetriol 26-monooxygenase, go to the full flat file.

Word Map on EC 1.14.15.15

Reaction

(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al
+ 2 reduced adrenodoxin + 2 H+ +
O2
=
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
+ 2 oxidized adrenodoxin +
H2O

Synonyms

5beta-cholestane-3 alpha,7alpha,12alpha,26-tetrol dehydrogenase, 5beta-cholestane-3 alpha,7alpha,12alpha-triol-26-al oxidoreductase, 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol 27-monooxygenase, 5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase, cholestanetriol 26-hydroxylase, cholestanetriol 27-hydroxylase, cholesterol C-26 hydroxylase, cholesterol hydroxylase, CYP125A4, CYP27, CYP27A, CYP27A1, cytochrome P-450 sterol 26-hydroxylase, cytochrome P-450A, cytochrome P450 125A4, cytochrome P450 27A, cytochrome P450c27, dehydrogenase, cholestanetetrol 26-, hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol, More, oxygenase, cholestanetriol 26-mono-, P450 27A1, sterol 27-hydroxylase, TEHC-NAD oxidoreductase, vitamin D3 25-hydroxylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.15.15 cholestanetriol 26-monooxygenase

Posttranslational Modification

Posttranslational Modification on EC 1.14.15.15 - cholestanetriol 26-monooxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease
side-chain modification
-
treatment of enzyme with iso[4]levuglandin E2 in vitro diminishes enzyme activity. Lys residues Lys134, Lys358, and Lys476, readily interact iso[4]levuglandin E2 in vitro, and modified CYP27A1 is present in the retina