Dephosphorylation of pig heart pyruvate dehydrogenase phosphate complexes by pig heart pyruvate dehydrogenase phosphate phosphatase [PDF]
Biochemical Journal, 1981 1. Pig heart pyruvate dehydrogenase phosphate complex in which all three sites of phosphorylation were completely phosphorylated was re-activated at a slower rate by phosphatase than complex predominantly phosphorylated in site 1. The ratio of initial rates of re-activation was approx.
A L Kerbey, P J Randle, A. Kearns
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Phosphorylation of additional sites on pyruvate dehydrogenase inhibits its re-activation by pyruvate dehydrogenase phosphate phosphatase [PDF]
Biochemical Journal, 1978 The phosphorylation of sites additional to an inactivating site inhibits the formation of active pig heart pyruvate dehydrogenase complex from inactive pyruvate dehydrogenase phosphate complex by pig heart pyruvate dehydrogenase phosphate phosphatase.
P H Sugden +3 more
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Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. [PDF]
Proceedings of the National Academy of Sciences, 1996 Bovine pyruvate dehydrogenase phosphatase (PDP) is a Mg2+-dependent and Ca2+-stimulated heterodimer that is a member of the protein phosphatase 2C family and is localized to mitochondria. Insight into the function of the regulatory subunit of PDP (PDPr) has been gained. It decreases the sensitivity of the catalytic subunit of PDP (PDPc) to Mg2+.
Yan Jin, Janet E. Lawson, Lester J. Reed
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Requirements for the Adaptor Protein Role of Dihydrolipoyl Acetyltransferase in the Up-regulated Function of the Pyruvate Dehydrogenase Kinase and Pyruvate Dehydrogenase Phosphatase [PDF]
Journal of Biological Chemistry, 1998 The dihydrolipoyl acetyltransferase (E2 component) is a 60-mer assembled via its COOH-terminal domain with exterior E1-binding domain and two lipoyl domains (L2 then L1) sequentially connected by mobile linker regions. E2 facilitates markedly enhanced function of the pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP ...
Da‐Qing Yang +3 more
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Purification of Bovine Kidney and Heart Pyruvate Dehydrogenaseb Phosphatase on Sepharose Derivatized with the Pyruvate Dehydrogenase Complex [PDF]
European Journal of Biochemistry, 1982 Pyruvate dehydrogenase phosphatase has been purified to apparent homogeneity from mitochondrial extracts of both beef heart and beef kidney. An essential step in this three-step purification is affinity chromatography of a largely purified phosphatase fraction using Sepharose beads to which pyruvate dehydrogenase complex is covalently bound through the
Mary L. Pratt +2 more
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Some Properties of Pea Mitochondrial Phospho-Pyruvate Dehydrogenase-Phosphatase [PDF]
Plant Physiology, 1987 Reactivation of the pea mitochondrial pyruvate dehydrogenase complex was the result of dephosphorylation catalyzed by phospho-pyruvate dehydrogenase-phosphatase, an intrinsic component of the complex. Phosphatase activity was dependent upon divalent metal ions, with Mg(2+) more effective than Mn(2+) or Co(2+). The Michaelis constants for Mg(2+), Mn(2+),
Ján A. Miernyk, Douglas D. Randall
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Crystal Structure of Pyruvate Dehydrogenase Phosphatase 1 and its Functional Implications [PDF]
Journal of Molecular Biology, 2007 Pyruvate dehydrogenase phosphatase 1 (PDP1) catalyzes dephosphorylation of pyruvate dehydrogenase (E1) in the mammalian pyruvate dehydrogenase complex (PDC), whose activity is regulated by the phosphorylation-dephosphorylation cycle by the corresponding protein kinases (PDHKs) and phosphatases.
Dmitry G. Vassylyev, J. Symerský
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Starvation and Diabetes Reduce the Amount of Pyruvate Dehydrogenase Phosphatase in Rat Heart and Kidney [PDF]
Diabetes, 2003 The pyruvate dehydrogenase complex (PDC) is inactivated in many tissues during starvation and diabetes to conserve three-carbon compounds for gluconeogenesis. This is achieved by an increase in the extent of PDC phosphorylation caused in part by increased pyruvate dehydrogenase kinase (PDK) activity due to increased PDK expression.
Boli Huang +3 more
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Metabolic and Biochemical Responses of Juvenile Babylonia areolata to Hypoxia Stress [PDF]
BiologyAs an important aquaculture species, the marine snail Babylonia areolata is frequently subjected to fluctuation in dissolved oxygen concentration during farming and transportation processes.
Baojun Tang +5 more
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Cloning, Expression, and Properties of the Regulatory Subunit of Bovine Pyruvate Dehydrogenase Phosphatase [PDF]
Journal of Biological Chemistry, 1997 cDNA encoding the regulatory subunit of bovine mitochondrial pyruvate dehydrogenase phosphatase (PDPr) has been cloned. Overlapping cDNA fragments were generated by the polymerase chain reaction from bovine genomic DNA and from cDNA synthesized from bovine poly(A)+ RNA and total RNA. The complete cDNA (2885 base pairs) contains an open reading frame of
Janet E. Lawson +4 more
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