Peroxisomal uptake of very long-chain fatty acyl CoA

Stable Identifier
R-HSA-390393
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
a very long-chain fatty acyl-CoA(out) + ATP + 2 H2O => a very long-chain fatty acid(in) + ADP + CoA + 2 H(+)
ReviewStatus
5/5
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ABCD1 (ATP-binding cassette sub-family D member 1) mediates the ATP-dependent, coupled peroxisomal import and hydrolysis of cytosolic very long chain fatty-acyl-CoA to form peroxisomal very long-chain fatty acid and CoASH (Kawaguchi et al. 2021; van Roermund et al. 2011; van Roermund et al. 2012).
Literature References
PubMed ID Title Journal Year
21145416 Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid β-oxidation

Wanders, RJ, IJlst, L, Visser, WF, van Roermund, CW, Waterham, HR

Biochim Biophys Acta 2011
33500543 Acyl-CoA thioesterase activity of peroxisomal ABC protein ABCD1 is required for the transport of very long-chain acyl-CoA into peroxisomes

Yamashita, A, So, T, Kawaguchi, K, Mukai, E, Morita, M, Imanaka, T, Watanabe, S

Sci Rep 2021
22493507 Peroxisomal fatty acid uptake mechanism in Saccharomyces cerevisiae

Wanders, RJ, Folkerts, H, IJlst, L, Hellingwerf, KJ, van Roermund, CW, Majczak, W, Waterham, HR

J Biol Chem 2012
Participants
Participates
Catalyst Activity

ATPase-coupled transmembrane transporter activity of ABCD1 homodimer [peroxisomal membrane]

Orthologous Events
Cross References
RHEA
Authored
Reviewed
Created
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