Cholesterol 25-hydroxylase

Cholesterol 25-hydroxylase
Cholesterol 25-hydroxylase
Identifiers
EC number 1.14.99.38
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a cholesterol 25-hydroxylase (EC 1.14.99.38) is an enzyme that catalyzes the chemical reaction

cholesterol + AH2 + O2 \rightleftharpoons 25-hydroxycholesterol + A + H2O

The 3 substrates of this enzyme are cholesterol, an electron acceptor AH2, and O2, whereas its 3 products are 25-hydroxycholesterol, the reduction product A, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is cholesterol, hydrogen-donor:oxygen oxidoreductase (25-hydroxylating). This enzyme is also called cholesterol 25-monooxygenase.

Transcripts for this enzyme have been identified in macrophages from the testis.

References

  • Lund EG, Kerr TA, Sakai J, Li WP, Russell DW (1998). "cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism". J. Biol. Chem. 273 (51): 34316–27. doi:10.1074/jbc.273.51.34316. PMID 9852097. 
  • Chen JJ, Lukyanenko Y, Hutson JC (2002). "25-hydroxycholesterol is produced by testicular macrophages during the early postnatal period and influences differentiation of Leydig cells in vitro". Biol. Reprod. 66 (5): 1336–41. doi:10.1095/biolreprod66.5.1336. PMID 11967195. 
  • Lukyanenko Y, Chen JJ, Hutson JC (2002). "Testosterone regulates 25-hydroxycholesterol production in testicular macrophages". Biol. Reprod. 67 (5): 1435–8. doi:10.1095/biolreprod.102.007575. PMID 12390873. 
  • Fox BG, Shanklin J, Ai J, Loehr TM, Sanders-Loehr J (1994). "Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins". Biochemistry. 33 (43): 12776–86. doi:10.1021/bi00209a008. PMID 7947683. 
  • Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annu. Rev. Biochem. 72: 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708. 
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