Open Accessα-KETO ACID DEHYDROGENASE COMPLEXES, X. REGULATION OF THE ACTIVITY OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM BEEF KIDNEY MITOCHONDRIA BY PHOSPHORYLATION AND DEPHOSPHORYLATION
Author(s) -
Tracy C. Linn,
Flora H. Pettit,
Lester J. Reed
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.62.1.234
Subject(s) - pyruvate dehydrogenase kinase , pyruvate dehydrogenase phosphatase , pyruvate dehydrogenase complex , pyruvate decarboxylation , dephosphorylation , oxoglutarate dehydrogenase complex , pyruvate dehydrogenase lipoamide kinase isozyme 1 , branched chain alpha keto acid dehydrogenase complex , dihydrolipoyl transacetylase , biochemistry , phosphorylation , chemistry , biology , phosphatase , dehydrogenase , enzyme
This paper reports the discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence. The site of this regulation is the pyruvate dehydrogenase component of the complex. Phosphorylation and concomitant inactivation of pyruvate dehydrogenase are catalyzed by an ATP-specific kinase (i.e., a pyruvate dehydrogenase kinase), and dephosphorylation and concomitant reactivation are catalyzed by a phosphatase (i.e., a pyruvate dehydrogenase phosphatase). The kinase and the phosphatase appear to be regulatory subunits of the pyruvate dehydrogenase complex.