Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
AEvarsson, A., Chuang, J.L., Wynn, R.M., Turley, S., Chuang, D.T., Hol, W.G.(2000) Structure 8: 277-291
- PubMed: 10745006 
- DOI: https://doi.org/10.1016/s0969-2126(00)00105-2
- Primary Citation of Related Structures:  
1DTW - PubMed Abstract: 
Mutations in components of the extraordinarily large alpha-ketoacid dehydrogenase multienzyme complexes can lead to serious and often fatal disorders in humans, including maple syrup urine disease (MSUD). In order to obtain insight into the effect of mutations observed in MSUD patients, we determined the crystal structure of branched-chain alpha-ketoacid dehydrogenase (E1), the 170 kDa alpha(2)beta(2) heterotetrameric E1b component of the branched-chain alpha-ketoacid dehydrogenase multienzyme complex.
Organizational Affiliation: 
Department of Biological Structure, University of Washington School of Medicine, Seattle 98195, USA.