Evidence that the mitochondrial activator of phosphorylated branched-chain 2-oxoacid dehydrogenase complex is the dissociated E1 component of the complex
- 25 June 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 172 (1) , 38-42
- https://doi.org/10.1016/0014-5793(84)80868-6
Abstract
Branched-chain 2-oxoacid dehydrogenase complex is inactivated by phosphorylation of the α-subunit of the E1 component of the complex. High-speed supernatant from rat liver mitochondria contains an activator protein which can restore activity to the phosphorylated complex without concomitant dephosphorylation [(1982) FEBS Lett. 147, 35–39]. We report here several lines of evidence which indicate that activator is the dissociated non-phosphorylated form of the E1 componentKeywords
This publication has 8 references indexed in Scilit:
- Multi‐site phosphorylation of branched‐chain 2‐oxoacid dehydrogenase complex within mitochondria isolated from rat liver, kidney and heartFEBS Letters, 1983
- Multi‐site phosphorylation of bovine kidney branched‐chain 2‐oxoacid dehydrogenase complexFEBS Letters, 1983
- Rapid purification of bovine kidney branched‐chain 2‐oxoacid dehydrogenase complex containing endogenous kinase activityFEBS Letters, 1983
- Stereoisomers of tetrahydrothiamin pyrophosphate, potent inhibitors of the pyruvate dehydrogenase multienzyme complex from Escherichia coliBiochemistry, 1983
- Activation of phosphorylated branched chain 2-oxoacid dehydrogenase complexFEBS Letters, 1982
- Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activityBiochemical Journal, 1982
- Inactivation of purified ox kidney branched‐chain 2‐oxoacid dehydrogenase complex by phosphorylationFEBS Letters, 1981
- Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidneyProceedings of the National Academy of Sciences, 1978