Back to Search
Start Over
Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH
- Source :
- FEBS Letters. 269:252-254
- Publication Year :
- 1990
- Publisher :
- Wiley, 1990.
-
Abstract
- Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed.
- Subjects :
- Physiological significance
Macromolecular Substances
Protein Conformation
Cooperativity
Allosteric regulation
Biophysics
Ketoglutarate dehydrogenase
Biochemistry
α-Ketoglutarate dehydrogenase
chemistry.chemical_compound
Protein structure
Allosteric Regulation
Structural Biology
Diethyl Pyrocarbonate
Genetics
Animals
Ketoglutarate Dehydrogenase Complex
Sulfhydryl Compounds
Columbidae
Molecular Biology
Dihydrolipoate
Thioctic Acid
Chemistry
Muscles
Substrate (chemistry)
Ketone Oxidoreductases
Cell Biology
NAD
Lipoic acid
NADH
Oxoglutarate dehydrogenase complex
Oxidation-Reduction
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 269
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....ca80f78ce18266402d64b394afd7a99f