Reactome | Arachidonate is hydroxylated to 19-HETE by CYP(2)

Arachidonate is hydroxylated to 19-HETE by CYP(2)

Stable Identifier

R-HSA-2161814

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, endoplasmic reticulum lumen

Synonyms

(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced (NADPH--hemoprotein reductase) => 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized (NADPH--hemoprotein reductase)

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Arachidonate is hydroxylated to 19-HETE by CYP(2)

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

Several cytochrome P450s (CYPs) convert arachidonate to 19-hydroxyeicosatetraenoic acid (19-HETE). The CYPs and their references are as follows: CYP2C8 (Bylund et al. 1998); CYP2C9 (Bylund et al. 1998); CYP2C19 (Bylund et al. 1998); CYP4A11 (Gainer et al. 2005); CYP2U1 (Chuang et al. 2004); CYP1A1, CYP1A2, CYP1B1 (Choudhary et al. 2004).

Literature References

PubMed ID	Title	Journal	Year
15611369	Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension Gainer, JV, Bellamine, A, Dawson, EP, Womble, KE, Grant, SW, Wang, Y, Cupples, LA, Guo, CY, Demissie, S, O'Donnell, CJ, Brown, NJ, Waterman, MR, Capdevila, JH	Circulation	2005
14660610	CYP2U1, a novel human thymus- and brain-specific cytochrome P450, catalyzes omega- and (omega-1)-hydroxylation of fatty acids Chuang, SS, Helvig, C, Taimi, M, Ramshaw, HA, Collop, AH, Amad, M, White, JA, Petkovich, M, Jones, G, Korczak, B	J Biol Chem	2004
15258110	Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1 Choudhary, D, Jansson, I, Stoilov, I, Sarfarazi, M, Schenkman, JB	Drug Metab Dispos	2004
9435160	Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes Bylund, J, Kunz, T, Valmsen, K, Oliw, EH	J Pharmacol Exp Ther	1998