Studies of Mammalian and Human Pyruvate and Alpha-Ketoglutarate Dehydrogenation Complexes.
Abstract
Enzyme systems that catalyze a coenzyme A- and nicotinamide adenine dinucleotide-linked oxidative decarboxylation of pyruvate and 2-oxoglutarate in mammals have been isolated from the Keilin-Hartree preparation of the pig heart muscle as soluble multi-enzyme complexes with molecular weights in the millions. The author's aims are to resolve these complexes into their essential enzymes, to characterize the latter, and to determine the composition, macromolecular structure and regulatory mechanism of these two multienzyme complexes. The pig heart pyruvate dehydrogenase complex has been successively separated into three component enzymes, (1) pyruvate dehydrogenase, (2) lipoate acetyltransferase, and (3) lipoamide dehydrogenase, and the complex has been reassembled from these isolated enzymes. The stoichiometry of the resolution and reconstitution of the mammalian multienzyme complex has been elucidated to a certain extent. The 2-oxoglutarate dehydrogenase complex has been separated into three component enzymes, (1) 2-oxoglutarate dehydrogenase, (2) lipoate succinyltransferase, and (3) lipoamide dehydrogenase, and the complex has been reassembled from these isolated enzymes. The stoichiometry of resolution and reconstitution of this complex has been shown in detail. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 01, 1972
- Accession Number
- AD0748120
Entities
People
- Masahiko Koike
Organizations
- Nagasaki University