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Evidence that the mitochondrial activator of phosphorylated branched‐chain 2‐oxoacid dehydrogenase complex is the dissociated E 1 component of the complex
Author(s) -
Yeaman Stephen J.,
Cook Kenneth G.,
Boyd Richard W.,
Lawson Rowena
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80868-6
Subject(s) - phosphorylation , activator (genetics) , dephosphorylation , protein subunit , chemistry , biochemistry , mitochondrion , pi , enzyme , microbiology and biotechnology , biology , phosphatase , gene
Branched‐chain 2‐oxoacid dehydrogenase complex is inactivated by phosphorylation of the α‐subunit of the E 1 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 E 1 component.