Kramlinger Valerie M, Nagy Leslie D, Fujiwara Rina, Johnson Kevin M, Phan Thanh T N, Xiao Yi, Enright Jennifer M, Toomey Matthew B, Corbo Joseph C, Guengerich Frederick Peter
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO, USA.
FEBS Lett. 2016 May;590(9):1304-12. doi: 10.1002/1873-3468.12167. Epub 2016 Apr 17.
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.
在人类中,皮肤中相当一部分类视黄醇库来源于维生素A2(全反式3,4-脱氢视黄醛)。维生素A2可能由角质形成细胞在局部产生,角质形成细胞在细胞培养中可将维生素A1(全反式视黄醇)转化为维生素A2。我们报告称,人类细胞色素P450(hP450)27C1,一种先前的“孤儿”酶,能够催化此反应。纯化的重组hP450 27C1可结合并使全反式视黄醇、视黄醛、视黄酸以及11-顺式视黄醛去饱和。尽管3,4-脱氢类视黄醇在人类中的生理作用尚不清楚,但我们已确定hP450 27C1是一种能够有效介导其形成的酶。