Very Long-chain Acyl-CoA Synthetase

Fatty acid transport protein paralogues 1-6 FATP 1-6 Gene symbols SLC27A1-6 Solute carrier family 27A Very long-chain acyl-CoA synthetase VLCS... 

Venus Flytrap Module Very Long-chain Acyl-CoA Synthetase Very Low-density Lipoprotein Vesicle... 

Herrmann, T., et al. Mouse fatty acid transport protein 4 (FATP4) characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase. Gene 2001, 270,... 

A separate very long-chain-acyl-CoA synthetase is present in peroxisomes for the activation of very long-chain fatty acids, such as arachidonate (20 carbon atoms). These fatty acids are degraded exclusively in the peroxisomes. 

Heinzer AK, Watkins PA, Lu IF, Kemp S, Moser AB, Li YY, MihaUk S, Powers JM, Smith KD. A very long-chain acyl-CoA synthetase-deficient mouse and its relevance to X-Unked adrenoleukodystrophy. Hum. Mol. Genet. 2003 12 1145-1154. 

Uchida Y, Kondo N, Orii T, Hashimoto T. Purification and properties of rat liver peroxisomal very-long-chain acyl-CoA synthetase. J Biochem 1996 119 565-71. 

Uchiyama, A., Aoyama, T., Kamijo, K., Uchida, Y, Kondo, N., Orii, T. Hashimoto, T. (19%) J. Biol. Chem. 271, 30360-30365. Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase. 

Lageweg, W Wanders, R. J. A. Tager, J. M. Long-chain-acyl-CoA synthetase and very-long-chain-acyl-CoA synthetase activities in peroxisomes and microsomes from rat liver. An enzymological study. But J. Biochem. 1991,196, 519-523. 

Like mitochondria, peroxisomes contain pathways for the /3-oxidation of fatty acids. The mechanism by which fatty acids enter peroxisomes is unclear but does not appear to involve the CPTl-CACT-CPT2 pathway. Long-chain and very-long-chain acyl-CoA synthetase activities are associated with peroxisomes, but it has not been established whether fatty acids or fatty acyl-CoAs traverse the peroxisomal membrane. The basic reactions of peroxisomal /3-oxidation resemble those found in mitochondria, but the peroxisomal and mitochondrial enzymes are distinct proteins (Figure 4). In fact, peroxisomes contain two sets of yS-oxidation enzymes, which appear to function with distinct substrates. 

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