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Gene Review

Acadvl  -  acyl-CoA dehydrogenase, very long chain

Rattus norvegicus

Synonyms: VLCAD, Very long-chain specific acyl-CoA dehydrogenase, mitochondrial, Vlcad
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Disease relevance of Acadvl

  • The VLCAD cDNA was expressed in four kinds of hepatoma cells using a vaccinia virus expression system and was shown to encode the catalytically active enzyme [1].
  • Loss in VLCAD activity during ischemia was not due to loss in protein content [2].
  • Thus, VLCAD represents a likely site for the modulation of substrate utilization during myocardial ischemia [2].

High impact information on Acadvl

  • The identity of the VLCAD clone was confirmed by matching the amino acid sequence predicted from the cDNA to the NH2 terminus and seven internal proteolytic peptide sequences from purified rat liver VLCAD [1].
  • Very long chain acyl-CoA dehydrogenase (VLCAD) activity declined 34% during 30 min of ischemia [2].
  • VLCAD, however, was active with CoA derivatives of long-chain saturated fatty acids or unsaturated fatty acids that have double bonds further removed from the thioester function [3].
  • The catalytic efficiency of rat VLCAD with 14:1 as substrate was only 4% of the efficiency determined with tetradecanoyl-CoA, whereas LCAD acted equally well on both substrates [3].
  • The CoA thioesters of docosahexaenoic acid, arachidonic acid, 4,7,10-cis-hexadecatrienoic acid, 5-cis-tetradecenoic acid, and 4-cis-decenoic acid were effectively dehydrogenated by both rat and human long-chain acyl-CoA dehydrogenases (LCAD), whereas they were poor substrates of very long-chain acyl-CoA dehydrogenases (VLCAD) [3].

Chemical compound and disease context of Acadvl

  • The cDNA expression in both rat hepatoma H4IIEC3 and McA-RH7777 enhanced about 3-fold mitochondrial beta-oxidation activity of long-chain fatty acids such as palmitic acid and stearic acid; hence, VLCAD is probably a rate-limiting enzyme in the long-chain fatty acid beta-oxidation system in these cell lines [1].


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