Results 201 to 210 of about 94,657 (246)

A mimic of the pyruvate dehydrogenase complex

Bioorganic & Medicinal Chemistry Letters, 2010
Pyruvic acid undergo decarboxylation catalyzed by a hydrophobic thiazolium salt and reacts with a hydrophobic analog of lipoic acid to form a hydrophobic acylthioester that reacts with aniline to form acetanilide in water, but only in the presence of a hydrophobically modified polyaziridine that acts to gather the reactants just as the enzyme complex ...
Huanyu, Zhao, Ronald, Breslow
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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
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Complexities of the pyruvate dehydrogenase complex

Neurology, 1998
If one were to throw a dart at the center of a biochemical chart for intermediary metabolism, it would land on acetyl-CoA. This metabolite is at the convergence of pyruvate, fatty acid, and ketone body metabolism. Condensation of acetyl-CoA with oxaloacetate forms citric acid, the entry point into the tricarboxylic acid cycle.
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The hormonal regulation of pyruvate dehydrogenase complex

Advances in Enzyme Regulation, 1996
The pyruvate dehydrogenase complex has a central role in the regulation of mammalian metabolism as it represents the point-of-no-return in the utilization of carbohydrate. This article summarizes our studies into how signalling systems initiated by hormones binding to cell surface receptors can reach the pyruvate dehydrogenase system which is located ...
Denton, RM, McCormack, JG, Rutter, GA, Burnett, Paul, Edgell, NJ, Moule, SK, Diggle, TA   +6 more
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Regulation of the Pyruvate Dehydrogenase Multienzyme Complex

Annual Review of Nutrition, 1993
To maximize catalytic efficiency in metabolic pathways of both prokaryotic and eUkaryotic cells, enzymatic components are occasionally clustered or complexed physically. Organization of multiple catalytic functions into a single enzyme complex can be accomplished in two ways.
R H, Behal, D B, Buxton, J G, Robertson, M S, Olson   +3 more
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Assays of Pyruvate Dehydrogenase Complex and Pyruvate Carboxylase Activity

2011
Pyruvate 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.
Douglas, Kerr, George, Grahame, Ghunwa, Nakouzi   +2 more
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Fluorescent derivatives of the pyruvate dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex

Biochemistry, 1977
One sulfhydryl group per polypeptide chain of the pyruvate dehydrogenase component of the pyruvate dehydrogenase multienzyme complex from Escherichia coli was selectively labeled with N-[P-(2-benzoxazoyl)phenyl]-maleimide (NBM), 4-dimethylamino-4-magnitude of-maleimidostilbene (NSM), and N-(4-dimethylamino-3,5-dinitrophenyl)maleimide (DDPM) in 0.05 M ...
N, Papadakis, G G, Hammes
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Structural diversity of pyruvate dehydrogenase complexes

FEBS Letters
The pyruvate dehydrogenase complex (PDHc) is a crucial metabolic enzyme complex found in all aerobic organisms. It catalyzes the conversion of pyruvate, the product of glycolysis, into acetyl‐CoA, a key substrate for the citric acid cycle and fatty acid synthesis.
Sarah N. Bothe, Rafal Zdanowicz
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Pyruvate Dehydrogenase Complex

1969
Publisher Summary This chapter discusses the multienzyme pyruvate dehydrogenase complexes, with emphasis on their structure, function, and regulation. These complexes have been isolated from Escherichia coli and from animal tissues as functional units with molecular weights in the millions.
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Regulation of the Human Pyruvate Dehydrogenase Complex

Clinical Science, 1976
1. 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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