The ACADVL gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase (VLCAD). This enzyme functions within mitochondria, the energy-producing centers in cells. Very long-chain acyl-CoA dehydrogenase is essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy.
Very long-chain acyl-CoA dehydrogenase is required to metabolize a group of fats called very long-chain fatty acids. These fatty acids are found in food and body fat. Fatty acids are a major source of energy for the heart and muscles. During periods without food (fasting), fatty acids are also an important energy source for the liver and other tissues.
Health Conditions Related to Genetic Changes
Very long-chain acyl-CoA dehydrogenase deficiency
More than 100 mutations in the ACADVL gene have been found to cause very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency. Many of these mutations change single protein building blocks (amino acids) in the VLCAD enzyme. Other mutations delete part of the ACADVL gene or create a premature stop signal in the instructions for making VLCAD. These mutations lead to a change in the enzyme's structure, severely reducing or eliminating its activity. As a result, very little functional enzyme is produced.
With a shortage (deficiency) of functional VLCAD enzyme, very-long chain fatty acids are not metabolized properly. As a result, these fats are not converted to energy, which can lead to signs and symptoms of this disorder such as the lack of energy (lethargy) and low blood sugar (hypoglycemia). Very long-chain fatty acids or partially metabolized fatty acids may build up in tissues and damage the heart, liver, and muscles. This abnormal buildup causes the other signs and symptoms of VLCAD deficiency.More About This Health Condition
Other Names for This Gene
- acyl-CoA dehydrogenase, very long chain
- acyl-coenzyme A dehydrogenase, very long chain
Additional Information & Resources
Tests Listed in the Genetic Testing Registry
Scientific Articles on PubMed
Catalog of Genes and Diseases from OMIM
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- Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J Clin Invest. 1995 Jun;95(6):2465-73. Citation on PubMed or Free article on PubMed Central
- Goetzman ES, Wang Y, He M, Mohsen AW, Ninness BK, Vockley J. Expression and characterization of mutations in human very long-chain acyl-CoA dehydrogenase using a prokaryotic system. Mol Genet Metab. 2007 Jun;91(2):138-47. Epub 2007 Mar 19. Citation on PubMed or Free article on PubMed Central
- Gregersen N, Andresen BS, Corydon MJ, Corydon TJ, Olsen RK, Bolund L, Bross P. Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. Hum Mutat. 2001 Sep;18(3):169-89. Review. Citation on PubMed
- Merritt JL 2nd, Matern D, Vockley J, Daniels J, Nguyen TV, Schowalter DB. In vitro characterization and in vivo expression of human very-long chain acyl-CoA dehydrogenase. Mol Genet Metab. 2006 Aug;88(4):351-8. Epub 2006 Apr 18. Citation on PubMed
- Pons R, Cavadini P, Baratta S, Invernizzi F, Lamantea E, Garavaglia B, Taroni F. Clinical and molecular heterogeneity in very-long-chain acyl-coenzyme A dehydrogenase deficiency. Pediatr Neurol. 2000 Feb;22(2):98-105. Citation on PubMed
- Souri M, Aoyama T, Hoganson G, Hashimoto T. Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane. FEBS Lett. 1998 Apr 17;426(2):187-90. Citation on PubMed
- Spiekerkoetter U, Sun B, Zytkovicz T, Wanders R, Strauss AW, Wendel U. MS/MS-based newborn and family screening detects asymptomatic patients with very-long-chain acyl-CoA dehydrogenase deficiency. J Pediatr. 2003 Sep;143(3):335-42. Citation on PubMed