Results 211 to 220 of about 124,495 (263)

The Pyruvate Dehydrogenase Multienzyme Complex

Angewandte Chemie International Edition in English, 1975
AbstractThe three enzymes pyruvate dehydrogenase, dihydrolipoamide transacetylase, and dihydrolipoamide dehydrogenase constitute the pyruvate dehydrogenase multienzyme complex of E. coli; in mammals the complex also contains a kinase and a phosphatase.
Ferdinand Hucho
exaly   +3 more sources

Peptides derived from pyruvate dehydrogenase as substrates for pyruvate dehydrogenase kinase and phosphatase

Biochemical and Biophysical Research Communications, 1977
Abstract Evidence is presented that phosphopeptides produced by tryptic digestion of phosphorylated pyruvate dehydrogenase are effective substrates for pyruvate dehydrogenase phosphatase and that the dephosphopeptides can serve as substrates for pyruvate dehydrogenase kinase.
Flora H Pettit, Lester J Reed, F H Pettit   +2 more
exaly   +3 more sources

Specificity of the pyruvate dehydrogenase kinase for pyruvate dehydrogenase component bound to the surface of the kidney pyruvate dehydrogenase complex and evidence for intracore migration of pyruvate dehydrogenase component

Biochemistry, 1983
Using the bovine kidney pyruvate dehydrogenase complex we have investigated the mechanism whereby about three pyruvate dehydrogenase (active form) kinase molecules, tightly bound to the dihydrolipoyl transacetylase core, can rapidly phosphorylate and inactivate about 20 pyruvate dehydrogenase (active form) (PDHa) tetramers which are also bound to the ...
D R, Brandt, T E, Roche
openaire   +2 more sources

Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex

Journal of Inherited Metabolic Disease, 1996
SummaryThe most common defect associated with deficiency of the pyruvate dehydrogenase (PDH) complex occurs in the E1 component, specifically due to mutations in the X‐linked E1α gene. Clinical sequelae of these mutations, which range from severe neonatal lactic acidosis to carbohydrate‐sensitive ataxia, can be different in males and females depending ...
B H, Robinson, N, MacKay, K, Chun, M, Ling   +3 more
openaire   +2 more sources

Disorders of the pyruvate dehydrogenase complex

Journal of Inherited Metabolic Disease, 1986
AbstractPyruvate dehydrogenase deficiency may be a non‐specific consequence of many different neurological degenerative disorders. There are also serious methodological problems in estimating the activity of this enzyme complex.
D, Stansbie, S J, Wallace, C, Marsac
openaire   +2 more sources

Inhibition of pyruvate dehydrogenase and pyruvate dehydrogenase phosphate phosphatase by glyoxylate

Bioorganic Chemistry, 1985
Abstract The overall reaction catalyzed by the pyruvate dehydrogenase complex from rat epididymal fat tissue is inhibited by glyoxylate at concentrations greater than 10 μ m . The inhibition is competitive with respect to pyruvate; Ki was found to be 80 μ m .
Susan M. Beatty, Gordon A. Hamilton
openaire   +1 more source

Pyruvate dehydrogenase deficiency and epilepsy

Brain and Development, 2011
The pyruvate dehydrogenase complex (PDHc) is a mitochondrial matrix multienzyme complex that provides the link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the conversion of pyruvate into acetyl-CoA. PDHc deficiency is one of the commoner metabolic disorders of lactic acidosis presenting with neurological phenotypes that vary
Chitra, Prasad, Tony, Rupar, Asuri N, Prasad   +2 more
openaire   +2 more sources

Regulation of mammalian pyruvate dehydrogenase

Molecular and Cellular Biochemistry, 1975
In mammalian tissues, two types of regulation of the pyruvate dehydrogenase complex have been described: end product inhibition by acetyl CoA and NADH: and the interconversion of an inactive phosphorylated form and an active nonphosphorylated form by an ATP requiring kinase and a specific phosphatase.
R M, Denton, P J, Randle, B J, Bridges, R H, Cooper, A L, Kerbey, H T, Pask, D L, Severson, D, Stansbie, S, Whitehouse   +8 more
openaire   +2 more sources

Regulation of the pyruvate dehydrogenase complex

Biochemical Society Transactions, 2006
The PDC (pyruvate dehydrogenase complex) plays a central role in the maintenance of glucose homoeostasis in mammals. The carbon flux through the PDC is meticulously controlled by elaborate mechanisms involving post-translational (short-term) phosphorylation/dephosphorylation and transcriptional (long-term) controls.
M S, Patel, L G, Korotchkina
openaire   +2 more sources