Cloning and characterization of a human cDNA ACAD10 mapped to chromosome 12q24.1

Mol Biol Rep. 2004 Sep;31(3):191-5. doi: 10.1023/b:mole.0000043622.57408.6b.

Abstract

Mitochondrial fatty acid beta-oxidation is an important energy resource for many mammal tissues. Acyl-CoA dehydrogenases (ACADs) are a family of flavoproteins that are involved in the beta-oxidation of the fatty acyl-CoA derivatives. Deficiency of these ACADs can cause metabolic disorders including muscle fatigue, hypoglycaemia, hepatic lipidosis and so on. By large scale sequencing, we identified a cDNA sequence of 3960 base pairs with a typical acyl-CoA dehydrogenase function domain. RT-PCR result shows that it is widely expressed in human tissues, especially high in liver, kidney, pancreas and spleen. It is hypothesized that this is a novel member of ACADs family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl-CoA Dehydrogenase / biosynthesis
  • Acyl-CoA Dehydrogenase / chemistry*
  • Acyl-CoA Dehydrogenase / genetics*
  • Acyl-CoA Dehydrogenases / chemistry
  • Acyl-CoA Dehydrogenases / genetics*
  • Amino Acid Sequence
  • Chromosomes, Human, Pair 12*
  • Computational Biology
  • DNA, Complementary / metabolism
  • Exons
  • Gene Library
  • Humans
  • Introns
  • Molecular Sequence Data
  • Oxygen / metabolism
  • Protein Structure, Tertiary
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Tissue Distribution

Substances

  • DNA, Complementary
  • Acyl-CoA Dehydrogenases
  • ACAD10 protein, human
  • Acyl-CoA Dehydrogenase
  • Oxygen

Associated data

  • GENBANK/AY323912