Results 201 to 210 of about 140,469 (257)
Molecular Ecology, EarlyView.ABSTRACT Adaptation to the environment plays an essential role in yeast evolution as a consequence of selective pressures. Lachancea thermotolerans, a yeast related to fermentation and one of the current trends in wine technology research, has undergone an anthropisation process, leading to a notable genomic and phenomic differentiation.
Javier Vicente +5 more
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Molecular Microbiology, EarlyView.COL is an unusual “model” strain of Staphylococcus aureus that exhibits slow growth and multidrug antibiotic tolerance. This phenotype is primarily due to a mutation in Prs, which synthesizes the core metabolite phosphoribosyl pyrophosphate (PRPP). Introduction of the COL Prs allele into the antibiotic‐susceptible strain Newman confers tolerance, while
Claire E. Stevens +5 more
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Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex [PDF]
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 ...
Mingfu Ling +3 more
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Regulation of the pyruvate dehydrogenase complex
Biochemical Society Transactions, 2006The 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.
Mulchand S. Patel +1 more
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Disorders of the pyruvate dehydrogenase complex
Journal of Inherited Metabolic Disease, 1986AbstractPyruvate 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
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A mimic of the pyruvate dehydrogenase complex
Bioorganic & Medicinal Chemistry Letters, 2010Pyruvic 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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Complexities of the pyruvate dehydrogenase complex
Neurology, 1998If 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 pyruvate dehydrogenase multienzyme complex
Current Opinion in Structural Biology, 1992Abstract During the review period, several structures of component enzymes and domains of enzymes of this multienzyme complex were determined. Three structures of the flavoprotein component, dihydrolipoamide dehydrogenase, became available. The structure of the core component, dihydrolipoyl acetyltransferase, can in principle be constructed from the ...
Richard N. Perham +2 more
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Regulation of the Pyruvate Dehydrogenase Multienzyme Complex
Annual Review of Nutrition, 1993To 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.
Denis B. Buxton +3 more
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