Reactome | CYP4V2 omega-hydroxylates DHA to HDoHE

CYP4V2 omega-hydroxylates DHA to HDoHE

Stable Identifier

R-HSA-6786239

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, cytosol

Synonyms

(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced (NADPH--hemoprotein reductase) => 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized (NADPH--hemoprotein reductase)

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The main physiological function of normal retinal photoreceptor epithelial (RPE) cells is to import polyunsaturated fatty acids (PUFAs) from the bloodstream and to recycle them to maintain lipid homeostasis in photoreceptors. CYP4 enzymes are microsomal fatty acid omega-hydroxylases that function to degrade cellular lipids. CYP4V2 is present in epithelial cells of the retina and cornea, localised to the endoplasmic reticulum membrane and can hydroxylate PUFAs to their respective omega-hydroxylated products. Docosahexaenoic acid (DHA), which is found at high concentrations in the eye, is a C22 PUFA which is hydroxylated to omega-hydroxy-DHA (Nakano et al. 2009, 2012). Defects in CYP4V2 can cause Bietti crystalline corneoretinal dystrophy (BCD; MIM:210370), an ocular disease characterised by retinal degeneration and marginal corneal dystrophy resulting in progressive night blindness and constriction of the visual field. A typical feature is multiple glistening intraretinal crystals scattered over the fundus (Li et al. 2004, Nakano et al. 2012).

Literature References

PubMed ID	Title	Journal	Year
19661213	Expression and characterization of CYP4V2 as a fatty acid omega-hydroxylase Nakano, M, Kelly, EJ, Rettie, AE	Drug Metab. Dispos.	2009
22772592	CYP4V2 in Bietti's crystalline dystrophy: ocular localization, metabolism of ω-3-polyunsaturated fatty acids, and functional deficit of the p.H331P variant Nakano, M, Kelly, EJ, Wiek, C, Hanenberg, H, Rettie, AE	Mol. Pharmacol.	2012
15042513	Bietti crystalline corneoretinal dystrophy is caused by mutations in the novel gene CYP4V2 Li, A, Jiao, X, Munier, FL, Schorderet, DF, Yao, W, Iwata, F, Hayakawa, M, Kanai, A, Shy Chen, M, Alan Lewis, R, Heckenlively, J, Weleber, RG, Traboulsi, EI, Zhang, Q, Xiao, X, Kaiser-Kupfer, M, Sergeev, YV, Hejtmancik, JF	Am J Hum Genet	2004

Participants

Input

Output

Participates

as an event of

Catalyst Activity

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen of CYP4V2 [endoplasmic reticulum membrane]

Physical Entity

CYP4V2 [endoplasmic reticulum membrane] (Homo sapiens)

Activity

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen (GO:0016709)

Orthologous Events

CYP4V2 omega-hydroxylates DHA to HDoHE (Bos taurus)

CYP4V2 omega-hydroxylates DHA to HDoHE (Caenorhabditis elegans)

CYP4V2 omega-hydroxylates DHA to HDoHE (Canis familiaris)

CYP4V2 omega-hydroxylates DHA to HDoHE (Danio rerio)

CYP4V2 omega-hydroxylates DHA to HDoHE (Drosophila melanogaster)

CYP4V2 omega-hydroxylates DHA to HDoHE (Gallus gallus)

CYP4V2 omega-hydroxylates DHA to HDoHE (Mus musculus)