Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene

✍ Scribed by K. Tanaka; I. Yokota; P. M. Coates; A. W. Strauss; D. P. Kelly; Z. Zhang; N. Gregersen; B. S. Andresen; Y. Matsubara; D. Curtis; Y.-T. Chen

• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 832 KB
• Volume: 1
• Category: Article
• ISSN: 1059-7794
• DOI: 10.1002/humu.1380010402

✦ Synopsis

Communicated by R.G. H. Cotton

Medium chain acyl-CoA dehydrogenase (MCAD) catalyzes the first reaction of the &oxidation cycle for 4-10-carbon fatty acids. MCAD deficiency is one of the most frequent inborn metabolic disorders in populations of northwestern European origin. In the compilation of data from a worldwide study of 172 unrelated patients each representing an independent pedigree, a total of 8 different mutations have been identified. Among them, a single prevalent mutation, 985A+G, was found in 90% of 344 variant alleles. 98sA-+G causes glutamate substitution for lysine-304 in the mature MCAD subunit, which causes impairment of tetramer assembly and instability of the protein. Three of 7 rarer mutations have been identified in a few unrelated patients, while the remaining 4 have each been found in only a single pedigree. In addition to tabulating the mutations, the acyl-CoA dehydrogenase gene family, the structure of the MCAD gene and the evolution of 985A-+G mutation are briefly discussed.