| Literature DB >> 6307746 |
H R Fatania, P A Patston, P J Randle.
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 degrees 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+ (K0.5 greater than 1 mM) and inhibited completely by 50 mM fluoride. Reactivation and dephosphorylation are attributed to a mitochondrial branched-chain dehydrogenase phosphatase.Entities:
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Year: 1983 PMID: 6307746 DOI: 10.1016/0014-5793(83)80585-7
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124