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FEBS Lett. 2016 May;590(9):1304-12. doi: 10.1002/1873-3468.12167. Epub 2016 Apr 17.

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

Author information

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.

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

PMID:
27059013
PMCID:
PMC4864060
DOI:
10.1002/1873-3468.12167
[Indexed for MEDLINE]
Free PMC Article

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