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Results for “LIPOAMIDE DEHYDROGENASE”

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PubMed1978

Lipoamide dehydrogenase regulation in rat brain.

The Pyruvate dehydrogenase multienzyme complex (PDHC) purified from rat brain is phosphorylated in the presence of low concentrations of ATP and MgCl2. The phosphorylated PDHC is incapable of catalyzing the oxidative decarboxylation of pyruvate. In the presence of high concentrations (10 mM) of MgCl2, the phosphorylated (inactive) PDHC is converted back to the dephospho-form of PDHC which is catalytically active. The dihydrolipoyl dehydrogenase (LAD) component, E3, of PDHC is inactivated by pyridoxal phosphate (PLP) and the PLP-inactivated LAD can be reactivated by an amino acid, taurine. These results indicate the reversible formation of Schiff base between PLP and LAD. They also provide clear evidence for the involvement of LAD (E3) in the previously reported inactivation of PDHC by PLP.

Adenosine Triphosphate↗
PubMed1979

Turnover of pegeon breast muscle pyruvate dehydrogenase complex.

The pigeon breast muscle pyruvate dehydrogenase complex was resolved into three component enzymes: lipoate acetyltransferase, pyruvate dehydrogenase, and lipoamide dehydrogenase. The antibodies against each component enzyme were prepared. All of the antibodies against component enzymes precipitated the pyruvate dehydrogenase complex. The enzyme complex was recovered as the immunoprecipitate from the extract of breast muscle of a pigeon that had received a single injection of L-[4,5-3H]leucine. The immunoprecipitate was separated into each component enzyme by SDS-polyacrylamide gel electrophoresis. The relative isotopic leucine incorporations per mg of protein into each component enzyme 4 h after the injection were 1.0 : 0.9 : 1.4 : 2.7 for lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase, respectively. The half-lives of lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase were 7.7, 2.5, 2.6, and 1.8 days, respectively. These results indicate that the component enzymes of the pyruvate dehydrogenase complex were synthesized and degraded at different rates.

Animals↗