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Regulation of mammalian pyruvate dehydrogenase kinase
Author(s) -
Popov Kirill M
Publication year - 1997
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/s0014-5793(97)01453-1
Subject(s) - pyruvate dehydrogenase phosphatase , pyruvate dehydrogenase complex , pyruvate dehydrogenase kinase , pyruvate dehydrogenase lipoamide kinase isozyme 1 , pyruvate decarboxylation , pyruvate kinase , pkm2 , dihydrolipoyl transacetylase , biochemistry , protein subunit , chemistry , branched chain alpha keto acid dehydrogenase complex , oxoglutarate dehydrogenase complex , biology , microbiology and biotechnology , enzyme , dehydrogenase , glycolysis , gene
It is generally believed that mammalian pyruvate dehydrogenase kinase is a heterodimer consisting of catalytic and regulatory subunits. However, the contribution of the two subunits to the kinase‐mediated signal transduction has remained undefined. In the present study recombinant components of mammalian pyruvate dehydrogenase complex were employed in order to characterize the role of the kinase catalytic subunit in the regulation of pyruvate dehydrogenase reaction. The results provide the first evidence strongly suggesting that the catalytic subunit of pyruvate dehydrogenase kinase is competent to respond to known effectors of kinase activity as well as to interact with the E 2 ‐core without assistance of a regulatory subunit.