Topic
Pyruvate dehydrogenase kinase
About: Pyruvate dehydrogenase kinase is a research topic. Over the lifetime, 4224 publications have been published within this topic receiving 161052 citations. The topic is also known as: [pyruvate dehydrogenase (lipoamide)] kinase & pyruvate dehydrogenase (lipoamide) kinase.
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TL;DR: Two additional phenotypes were observed in the Pdh-mutants: a reduced growth rate in glucose medium which was partially complemented by the amino acid leucine; and an increase in formation of petites which lack mitochondrial DNA [rho0], during growth on glucose, shown to be a result of inactivation of the PDA1 gene.
Abstract: Pyruvate dehydrogenase mutants of Saccharomyces cerevisiae were isolated by disruption of the PDAl gene. To this end, the PDAl gene encoding the E1α subunit of the pyruvate dehydrogenase complex was replaced by the dominant Tn5ble marker. Disruption of the PDAl gene abolished production of the E1α subunit and pyruvate dehydrogenase activity. Two additional phenotypes were observed in the Pdh− mutants: (a) a reduced growth rate in glucose medium which was partially complemented by the amino acid leucine; (b) an increase in formation of petites which lack mitochondrial DNA [rho°], during growth on glucose. Both phenotypes were shown to be a result of inactivation of the PDAl gene. Explanations for these phenotypes are discussed.
53 citations
TL;DR: Results suggest that substrate inhibition may be operative in vivo with the H-type lactate dehydrogenase and with the M-type enzyme.
Abstract: Lactate dehydrogenases at physiological concentrations are inhibited by high concentrations of pyruvate when the enzyme and the pyruvate are incubated in the presence of oxidized nicotinamide-adenine dinucleotide before assay. The inhibition is much more pronounced with the H-type than with the M-type lactate dehydrogenase. These results suggest that substrate inhibition may be operative in vivo.
53 citations
TL;DR: Human-mouse somatic cell hybrids have been isolated and examined for enzyme and chromosome constitution and evidence predicated on the absence of chromosomal rearrangements is provided for the lack of genetic linkage in the human genome for these four enzymes.
Abstract: Human-mouse somatic cell hybrids have been isolated and examined for enzyme and chromosome constitution. The enzymes assayed were lactate dehydrogenase (LDH), isocitrate dehydrogenase (IDH), NADP-dependent malate dehydrogenase (MDH), glucose 6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), phosphoglucomutase (PGM), and several esterases. Coexpression of mouse and human genomes and formation of heteropolymeric enzymes were observed in seven different hybrid populations for the enzymes LDH, IDH, MDH, and G6PD. Evidence predicated on the absence of chromosomal rearrangements is provided for the lack of genetic linkage in the human genome for these four enzymes, as well as for thymidine kinase.
53 citations
TL;DR: Pyruvate carboxylases isolated from the livers of rats, chickens, and sheep were shown to catalyze the fixation of H14CO3- in the absence of acetyl-CoA and to be dependent upon the enzyme concentration in the assay solution.
53 citations
TL;DR: Evidence that five lactate dehydrogenase isoenzymes vary in the ratio of LDH activity (pyruvate → lactate) to LDHActivity (lactate → pyruvates) is presented.
Abstract: Five lactate dehydrogenaseisoenzymesare normally observed in human serum: H4 (LDH1), H3M (LDH2), H2M2 (LDH3), HM3 (LDH4), and M4 (LDH5). This study presents evidence that these isoenzymesvary in the ratio of LDH activity (pyruvate-* lactate) to LDH activity (lactate -* pyruvate).
53 citations