Structural Basis of the Dysfunctioning of Human 2-Oxo Acid Dehydrogenase Complexes
Currently a wealth of both genetic and structural information is available. Three-dimensional structures of three components of the complex are presently available: of the pyruvate dehydrogenase component (E1), of the dihydrolipoyl acyltransferase component (E2) and of the lipoamide dehydrogenase component (E3). Moreover, detailed information on the reaction mechanism, regulation and the interactions between the different components of the complex is now at hand. Although only one of the structures is of human origin (E1b), model building by homology modelling allows us to investigate the causes of dysfunction.
In this review we have combined this knowledge to gain more insight into the structural basis of the dysfunctioning of the 2-oxo acid dehydrogenase complexes.
Keywords: Alzheimer disease; Chloramphenicol acetyltransferase; Dihydrolipoamide dehydrogenase component; Human 2-Oxo Acid Dehydrogenase; Maple Syrup; Protein-Protein Interactions; Transketolase; amino-pyrimidine moiety; dihydrolipoamide dehydrogenase component (E3); heterotetrameric
Document Type: Review Article
Publication date: February 1, 2002
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