Reactome | DECR2 reduces a (2E,4E)-dienoyl-CoA to a 4,5-saturated-(3E)-enoyl-CoA

DECR2 reduces a (2E,4E)-dienoyl-CoA to a 4,5-saturated-(3E)-enoyl-CoA

Stable Identifier

R-HSA-6786720

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix, peroxisomal membrane

Synonyms

a (2E,4E)-dienoyl-CoA + H(+) + NADPH => a 4,5-saturated-(3E)-enoyl-CoA + NADP(+)

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

DECR2 reduces a (2E,4E)-dienoyl-CoA to a 4,5-saturated-(3E)-enoyl-CoA

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

Saturated and unsaturated fats can undergo beta-oxidation in the mitochondrion and peroxisomes. The only major difference known so far is that peroxisomes can process linear as well as branched unsaturated fatty acid enoyl-CoA esters with much longer chains (>C20) when compared with the mitochondrion. Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) mediates the reduction of long-chain enoyl-CoA esters (2,3-dienoyl-CoA) to form 4,5-saturated-(3E)-enoyl-CoA esters (De Nys et al. 2001, Hua et al. 2012). DECR2 functions as an auxiliary enzyme for fatty acid beta-oxidation where very long-chain and long-chain fatty acids are shortened in peroxisomes and shuttled to the mitochondrion for complete degradation.

Literature References

PubMed ID	Title	Journal	Year
22745130	Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal β-oxidation of unsaturated fatty acids Shaw, N, Wang, J, Liu, ZJ, Wu, D, Hua, T, Ding, W	J. Biol. Chem.	2012
11514237	Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase De Nys, K, Van Veldhoven, PP, Fransen, M, Meyhi, E, Mannaerts, GP	Biochim. Biophys. Acta	2001