ELOVL1,4 elongate TCS-CoA and Mal-CoA to 3OHC-CoA

Stable Identifier
R-HSA-548830
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
lignoceroyl-CoA + malonyl-CoA => 3-oxocerotoyl-CoA + CO2 + CoASH
Locations in the PathwayBrowser
General
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

Elongation of very long chain fatty acids proteins 1, 4 (ELOVL1,4) catalyse the elongation of lignoceroyl-CoA (TCS-CoA) and malonyl-CoA (Mal-CoA) to form 3-oxocerotoyl-CoA (3OHC-CoA). ELOVL4 is abundant in retinal cells, where it is localized to the endoplasmic reticulum membrane (Grayson & Molday 2005). The catalytic activity of ELOVL4 has not been examined directly but is inferred from that of the homologous mouse protein, which is also active on polyunsaturated fatty acids (PUFAs) (PUFAs) (Agbada et al. 2008).

Literature References
PubMed ID Title Journal Year
18728184 Role of Stargardt-3 macular dystrophy protein (ELOVL4) in the biosynthesis of very long chain fatty acids

Agbaga, MP, Brush, RS, Mandal, MN, Henry, K, Elliott, MH, Anderson, RE

Proc Natl Acad Sci U S A 2008
16036915 Dominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4

Grayson, C, Molday, RS

J Biol Chem 2005
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
fatty acid elongase activity of ELOVL1,4 [endoplasmic reticulum membrane]
Physical Entity
Activity
Inferred From
Cross References
Rhea
Authored
Reviewed
Created
Cite Us!