Article
An unassembled subunit of NAD(+)-dependent isocitrate dehydrogenase is insoluble and covalently modified.
Archives of biochemistry and biophysics - 1 Jun 1998
Gadde D M, Yang E, McCammon M T
Abstract excerpt
The NAD(+)-dependent isocitrate dehydrogenase of Saccharomyces cerevisiae is an octamer composed of four Idh1p subunits and four Idh2p subunits. Isocitrate dehydrogenase functions in the tricarboxylic acid cycle and has also been reported to bind to the 5' nontranslated region of mitochondrially encoded mRNAs. Mutants defective in either or both of these subunits are unable to grow on the nonfermentable carbon...
Topics
- Fungal Proteins
- Isocitrate Dehydrogenase
- Macromolecular Substances
- Mitochondria
- Molecular Weight
- Mutation
- Oxidation-Reduction
- Protein Binding
- Protein Processing, Post-Translational
- Saccharomyces cerevisiae
- Solubility
