Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex.
In human (h) pyruvate dehydrogenase complex (PDC) the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). The C-terminal surface of the E1beta subunit was scanned for the negatively charged residues involved in binding with E2. betaD289 of hE1 interacts with K276 of hE2 in a manner similar to the corresponding interaction in Bacillus stearothermophilus PDC. In contrast to bacterial E1beta, the C-terminal residue of the hE1beta does not participate in the binding with positively charged residues of hE2. This latter finding shows species specificity in the interaction between hE1beta and hE2 in PDC.
Korotchkina
Lioubov G
LG
Department of Biochemistry, School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY 14214, USA.
Patel
Mulchand S
MS
D001665:Binding Sites; D006801:Humans; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D050505:Mutant Proteins; D011768:Pyruvate Dehydrogenase Complex; D007658:Ketone Oxidoreductases; C053164:pyruvate dehydrogenase (NADP+)