2. Academic Validation
  3. Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids

Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids

  • FEBS Lett. 2016 May;590(9):1304-12. doi: 10.1002/1873-3468.12167.
Valerie M Kramlinger 1,  Leslie D Nagy 1,  Rina Fujiwara 1,  Kevin M Johnson 1,  Thanh T N Phan 1,  Yi Xiao 1,  Jennifer M Enright 2,  Matthew B Toomey 2,  Joseph C Corbo 2,  Frederick Peter Guengerich 1
Affiliations

Affiliations

  • 1 Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
  • 2 Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO, USA.
PMID: 27059013 DOI: 10.1002/1873-3468.12167
Abstract

In humans, a considerable fraction of the retinoid pool in skin is derived from vitamin A2 (all-trans 3,4-dehydroretinal). Vitamin A2 may be locally generated by keratinocytes, which can convert vitamin A1 (all-trans retinol) into vitamin A2 in Cell Culture. We report that human Cytochrome P450 (hP450) 27C1, a previously 'orphan' Enzyme, can catalyze this reaction. Purified recombinant hP450 27C1 bound and desaturated all-trans retinol, retinal, and retinoic acid, as well as 11-cis-retinal. Although the physiological role of 3,4-dehydroretinoids in humans is unclear, we have identified hP450 27C1 as an Enzyme capable of efficiently mediating their formation.

Keywords

Cytochrome P450; desaturation; mass spectrometry; retinoids; spectroscopy.

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