Dephosphorylation and reactivation of phosphorylated purified ox‐kidney branched‐chain dehydrogenase complex by co‐purified phosphatase
- 25 July 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 158 (2), 234-238
- https://doi.org/10.1016/0014-5793(83)80585-7
Abstract
The branched-chain 2 oxoacid dehydrogenase complex has been purified from well-washed ox-kidney mitochondria together with branched-chain dehydrogenase kinase. The complex was inactivated and phosphorylated by ATP in about 5 min at 30°C. After hydrolysis of ATP by a contaminating ATPase (5–10 min) the complex was dephosphorylated and reactivated. Dephosphorylation and reactivation were linearly correlated. Reactivation was dependent upon Mg2+ (K 0.5 > 1 mM) and inhibited completely by 50 mM fluoride. Reactivation and dephosphorylation are attributed to a mitochondrial branched-chain dehydrogenase phosphatase.Keywords
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