Relevant conflicts of interest/financial disclosures: Sylvain Chouinard has consulted and served on the advisory board of Teva, AbbVie, Novartis, UBC and Allergan and has received honoraria from Teva, AbbVie, Novartis and UBC. Geneviéve Bernard has served as a consultant for Actelion Pharmaceuticals.
A treatable new cause of chorea: Beta-ketothiolase deficiency
Version of Record online: 1 JUL 2013
© 2013 Movement Disorder Society
Volume 28, Issue 8, pages 1054–1056, July 2013
How to Cite
Buhaş, D., Bernard, G., Fukao, T., Décarie, J.-C., Chouinard, S. and Mitchell, G. A. (2013), A treatable new cause of chorea: Beta-ketothiolase deficiency. Mov. Disord., 28: 1054–1056. doi: 10.1002/mds.25538
Full author roles may be found in the Acknowledments section online.
- Issue online: 12 AUG 2013
- Version of Record online: 1 JUL 2013
- Manuscript Accepted: 27 MAR 2013
- Manuscript Revised: 18 FEB 2013
- Manuscript Received: 5 OCT 2012
Additional Supporting Information may be found in the online version of this article.
|mds25538-sup-0001-suppfig1.eps||694K||Supplementary Figure 1. Isoleucine and ketone body metabolism. Mitochondrial acetoacetyl-coenzyme A (CoA) thiolase (beta-ketothiolase [T2]) is implicated in the metabolism of ketone bodies and of the amino acid isoleucine. (Left) Ketone body use in extrahepatic tissues is illustrated. (Right) T2 catalyzes the final reaction of isoleucine degradation. The preceding enzyme, 2-methylhydroxybutyryl-CoA dehydrogenase (MHBD), is shown. The metabolites present in T2 and MHBD deficiencies (boxes) are indicated to the right of each enzyme. SCOT indicates 3-ketoacid CoA transferase.|
|mds25538-sup-0002-suppvideo1.MP4||74577K||Supplementary Information Video|
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.