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Assays of Pyruvate Dehydrogenase Complex and Pyruvate Carboxylase Activity
2011Pyruvate dehydrogenase complex (PDC) and pyruvate carboxylase (PC) are mitochondrial enzymes that provide the initial steps of the two main alternatives for pyruvate metabolism: oxidative decarboxylation vs. anaplerotic carboxylation, gluconeogenesis, and glycerogenesis.
Ghunwa Nakouzi +2 more
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Regulation of the Human Pyruvate Dehydrogenase Complex
Clinical Science, 19761. The pyruvate dehydrogenase complex from human heart has been partially purified and shown to be regulated by a phosphorylation-dephosphorylation cycle similar to that previously found for other mammalian tissues. 2. Incubation of the complex with ATP (2 mmol/l) led to its inactivation associated with the concomitant incorporation into
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[66] Pyruvate dehydrogenase complex from Neurospora
1982Publisher Summary This chapter discusses the assay method, purification procedures, and properties of pyruvate dehydrogenase complex (PDC) isolated from Neurospora. The pyruvate dehydrogenase complex (PDC) is isolated from a number of sources, including Escherichia coli and other bacteria, the pigeon muscle, mammalian tissues Neurospora crassa, and ...
Dina F. Caroline +2 more
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Purification and properties of the Ascaris pyruvate dehydrogenase complex
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979The pyruvate dehyhdrogenase complex (pyruvate:lipoate oxidoreductase (decarboxylating and acceptor-acetylating), EC 1.2.4.1) has been isolated from Ascaris muscle mitochondria and purified to near homogeneity by differential centrifugation, (NH4)2SO4 fractionation and calcium phosphate gel-cellulose chromatography.
Howard J. Saz +2 more
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The Pyruvate Dehydrogenase Complex as a Target for Gene Therapy
Current Gene Therapy, 2003Here we review the rationale for considering the pyruvate dehydrogenase multienzyme complex (PDC) as a target for gene therapy for defects in mitochondrial energetics. PDC is entirely nuclear encoded and is situated in the mitochondrial inner membrane.
Renius Owen +2 more
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[67] Pyruvate dehydrogenase complex from Escherichia coli
1982Publisher Summary This chapter describes the assay method and purification procedures of pyruvate dehydrogenase complex isolated from Escherichia coli . The pyruvate dehydrogenase complex of E. coli consists of multiple copies of pyruvate decarboxylase and lipoamide dehydrogenase, which bind independently to dihydrolipoamide acetyltransferase.
Visser, J., Strating, M.
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Characterization of the inhibition of Escherichia coli pyruvate dehydrogenase complex by pyruvate
Biochemical and Biophysical Research Communications, 1991The E. coli pyruvate dehydrogenase complex was inhibited by pyruvate in absence of its cofactor, NAD+. The inhibition was found to increase with pH and phosphate concentration of the buffer and decrease with its ionic strength. The inhibition profile was different with MOPS buffer. No radioactivity was found in the enzyme, when the latter was incubated
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Human defects of the pyruvate dehydrogenase complex
1996Deficiency of the pyruvate dehydrogenase complex (PDC), a critical enzyme of energy metabolism, would appear incompatible with survival, particularly in the intrauterine environment where energy production depends primarily on glucose oxidation.
Isaiah D. Wexler +3 more
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Radiation therapy‐associated toxicity: Etiology, management, and prevention
Ca-A Cancer Journal for Clinicians, 2021Kyle Wang
exaly
The biochemistry of the pyruvate dehydrogenase complex*
Biochemistry and Molecular Biology Education, 2003Mulchand S. Patel +1 more
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