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Human Cytochrome P450 27C1 Catalyzes 3,4-Desaturation of Retinoids.

Research paper by Valerie M VM Kramlinger, Leslie D LD Nagy, Rina R Fujiwara, Kevin M KM Johnson, Thanh T N TT Phan, Yi Y Xiao, Jennifer M JM Enright, Matthew B MB Toomey, Joseph C JC Corbo, F Peter FP Guengerich

Indexed on: 10 Apr '16Published on: 10 Apr '16Published in: FEBS Letters



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. This article is protected by copyright. All rights reserved.