HRASLS transfer acyl group from PC to PE to form NAPE

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
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 H-RAS-like suppressor (HRASLS) subfamily consists of five enzymes (1–5) in humans that share sequence homology with lecithin:retinol acyltransferase (LRAT). All HRASLS members possess in vitro phospholipid metabolizing abilities including phospholipase A1/2 (PLA1/2) activities and O-acyltransferase activities for the remodeling of glycerophospholipid acyl chains (Golczak et al. 2012), as well as N-acyltransferase activities for the production of N-acylphosphatidylethanolamines (Mardian et al. 2015). Acyl chain remodelling can play a key role in regulating triglyceride accumulation and energy expenditure in adipocytes, making this process a potential target for treatment of metabolic disorders causing obesity. The example here describes the N-acyltransferase activity of HRASLSs for the production of N-acylphosphatidylethanolamines (NAPEs) (Uyama et al. 2012).
Literature References
PubMed ID Title Journal Year
26503625 The HRASLS (PLA/AT) subfamily of enzymes

Mardian, EB, Duncan, RE, Bradley, RM

J. Biomed. Sci. 2015
22825852 Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family

Shinohara, N, Uyama, T, Jin, XH, Tonai, T, Ueda, N, Tsuboi, K, Tokumura, A, Inoue, M, Ikematsu, N

J. Biol. Chem. 2012
22605381 Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins

Sears, AE, Kiser, PD, Blaner, WS, Golczak, M, Palczewski, K, Lodowski, DT

J. Biol. Chem. 2012
Catalyst Activity

acyltransferase activity of HRASLS [cytosol]

Orthologous Events
Cite Us!