@article{b361412ec63346d9b1c2c14d1ea6a468,
title = "Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids",
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",
author = "Kramlinger, {Valerie M.} and Nagy, {Leslie D.} and Rina Fujiwara and Johnson, {Kevin M.} and Phan, {Thanh T.N.} and Yi Xiao and Enright, {Jennifer M.} and Toomey, {Matthew B.} and Corbo, {Joseph C.} and Guengerich, {Frederick Peter}",
note = "Funding Information: This work was supported by United States National Institutes of Health grants R37 CA090426 (F.P.G.), EY026672 (J.C.C.), EY024958 (J.C.C.), T32 ES007028 (V.M.K.), T32 CA009582 (K.M.J.), T32 EY013360 (J.M.E., M.B.T), and F31 NS083170 (J.M.E.), the National Science Foundation DBI1202776 (M.B.T.), and the Human Frontier Science Program (J.C.C.). We thank K. Trisler for her assistance in preparation of the manuscript. Publisher Copyright: {\textcopyright} 2016 Federation of European Biochemical Societies.",
year = "2016",
month = may,
day = "1",
doi = "10.1002/1873-3468.12167",
language = "English",
volume = "590",
pages = "1304--1312",
journal = "FEBS Letters",
issn = "0014-5793",
number = "9",
}