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

Kramlinger VM, Nagy LD, Fujiwara R, Johnson KM, Phan TT, Xiao Y, Enright JM, Toomey MB, Corbo JC, Guengerich FP
FEBS Lett. 2016 590 (9): 1304-12

PMID: 27059013 · PMCID: PMC4864060 · DOI:10.1002/1873-3468.12167

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.

© 2016 Federation of European Biochemical Societies.

MeSH Terms (3)

Cytochrome P450 Family 27 Humans Retinoids

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