Pyruvate Dehydrogenase Phosphatase Deficiency [PDF]
Pediatric Research, 1975 A male child presented on the first day of life with metabolic acidosis with elevated blood lactate (15 mM), pyruvate (0.4 mM), and free fatty acid (1.3 mM) levels and a blood pH of 7.16. The severity of the acidosis was diminished by intravenous administration of glucose in large doses and by bicarbonate.
B H, Robinson, W G, Sherwood
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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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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
M L, Pratt, J F, Maher, T E, Roche
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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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Activation of pyruvate dehydrogenase in adipose tissue by insulin. Evidence for an effect of insulin on pyruvate dehydrogenase phosphate phosphatase [PDF]
Biochemical Journal, 1975 1. The mechanism by which insulin activates pyruvate dehydrogenase in rat epididymal adipose tissue was further investigated. 2. When crude extracts, prepared from tissue segments previously exposed to insulin (2m-i.u/ml) for 2min, were supplemented with Mg-2+, Ca-2+, glucose and hexokinase and incubated at 30 degrees C, they displayed an enhanced rate
C, Mukherjee, R L, Jungas
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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+.
J, Yan, J E, Lawson, L J, Reed
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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+),
J A, Miernyk, D 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, Jindrich, Symersky
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Isoenzymes of Pyruvate Dehydrogenase Phosphatase [PDF]
Journal of Biological Chemistry, 1998 Boli Huang +5 more
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Sub‐mitochondrial localization of the catalytic subunit of pyruvate dehydrogenase phosphatase [PDF]
FEBS Letters, 1997 Using a specific antibody against the PDP catalytic subunit, PDPc, precise localization of this subunit in mitochondria was performed. Sub‐fractionation of purified mitochondria by controlled swelling processes led to the isolation of outer membranes, matrix space and inner membrane vesicles which were purified on a sucrose density gradient.
Simonot, Cédric +3 more
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