5-HEDH dehydrogenates 5-HEPE to 5-oxo-EPA

Stable Identifier
R-HSA-9027632
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, endoplasmic reticulum membrane
ReviewStatus
5/5
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5-HEDH dehydrogenates 5-HEPE to 5-oxo-EPA
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In neutrophils, 5-hydroxyeicosanoid dehydrogenase (5-HEDH) activity is localised in the microsomal fraction and requires NADP+ as a cofactor to oxidise 5-hydroxy-eicosapentaenoic acid (5-HEPE) to 5-oxo-eicosapentaenoic acid (5-oxo-EPA) (Powell et al. 1995, Patel et al. 2009). Although 5-HEDH activity has been found in a wide range of intact cells and in crude microsome preparations, the enzyme has not yet been purified, its structure is unknown, and the gene that encodes it remains to be identified. Dietary EPA supplementation significantly increases the formation of 5-oxo-EPA that transduces anti-inflammatory actions rather than suppressing production of pro-inflammatory AA metabolites (Cipollina et al. 2014).
Literature References
PubMed ID Title Journal Year
24736647 Generation and dietary modulation of anti-inflammatory electrophilic omega-3 fatty acid derivatives

Cipollina, C, Salvatore, SR, Muldoon, MF, Freeman, BA, Schopfer, FJ

PLoS ONE 2014
8847485 Formation of a 5-oxo metabolite of 5,8,11,14,17-eicosapentaenoic acid and its effects on human neutrophils and eosinophils

Powell, WS, Gravel, S, Gravelle, F

J. Lipid Res. 1995
19164464 Substrate selectivity of 5-hydroxyeicosanoid dehydrogenase and its inhibition by 5-hydroxy-Delta6-long-chain fatty acids

Patel, P, Cossette, C, Anumolu, JR, Erlemann, KR, Grant, GE, Rokach, J, Powell, WS

J. Pharmacol. Exp. Ther. 2009
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Output
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Catalyst Activity

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor of 5-HEDH [endoplasmic reticulum membrane]

Physical Entity
5-HEDH [endoplasmic reticulum membrane] (Homo sapiens)
Activity
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)
Authored
Jassal, B  (2017-11-03)
Reviewed
Hansen, TV  (2018-02-21)
Created
Jassal, B  (2017-11-03)
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