Pyruvate Decarboxylase
Mostrando 1-12 de 125 artigos, teses e dissertações.
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1. Waterlogging-induced changes in fermentative metabolism in roots and nodules of soybean genotypes
Waterlogging blocks the oxygen supply to the root system which inhibits respiration, and greatly reduces the energy status of cells that affect important metabolic processes. This study evaluated fermentative metabolism and carbohydrate contents in the root system of two soybean (Glycine max L. Merril) genotypes under hypoxic and post-hypoxic conditions. Nod
Sci. agric. (Piracicaba, Braz.). Publicado em: 2014-12
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2. Phytomonas serpens: caracterização da piruvato/indolpiruvato descarboxilase e funcionalidade da auxina produzida. / Phytomonas serpens: characterization of the pyruvate/indolepyruvate decarboxylase and functionality of the auxin produced.
Um gene que codifica uma piruvato/indolpiruvato descarboxilase (PDC/IPDC) está presente no tripanossomatídeo de plantas Phytomonas serpens. A PDC atua na fermentação alcoólica, enquanto que a IPDC atua na biossíntese do fitormônio ácido indol-3-acético (AIA). Análises filogenéticas indicam que a PDC/IPDC de P. serpens é monofilética com IPDCs de
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 22/05/2012
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3. Metabolismo de lactose em Kluyveromyces marxianus UFV-3 e Kluyveromyces lactis JA6 / Metabolism of lactose by Kluyveromyces marxianus UFV-3 and Kluyveromyces lactis JA6
The fermentative metabolism of lactose in Kluyveromyces marxianus UFV-3 was compared to the Kluyveromyces lactis JA6 under aerobic and hypoxia through the analysis of kinetics of growth, consumption of substrate, production of ethanol and formation of biomass, depending on the concentration of lactose. It was determinated the gene expression and activity of
Publicado em: 2009
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4. Analise da estrutura de piruvato descarboxilase de Saccharomyces cerevisiae MC 16
t: Pyruvate decarboxylase (PDC, EC 4.1.1.1) is a key enzyme in the yeast carbon metabolism, driving pyruvic acid towards ethanol production. Although it is well established that the enzyme is a tetramer of about 240 KD, its monomeric subunit structure is still a matter of controversy. Either one or two subunit types have been described and three structural g
Publicado em: 1993
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5. Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis.
Six different pyruvate decarboxylase mutants of Saccharomyces cerevisiae were isolated. They belong to two unlinked complementation groups. Evidence is presented that one group is affected in a structural gene. The fact that five of the six mutants had residual pyruvate decarboxylase activity provided the opportunity for an intensive physiological characteri
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6. Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae.
Pyruvate decarboxylase is the key enzyme in alcoholic fermentation in yeast. Two structural genes, PDC1 and PDC5 have been characterized. Deletion of either of these genes has little or no effect on the specific pyruvate decarboxylase activity, but enzyme activity is undetectable in mutants lacking both PDC1 and PDC5 (S. Hohmann and H. Cederberg, Eur. J. Bio
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7. Promoter and nucleotide sequences of the Zymomonas mobilis pyruvate decarboxylase.
DNA sequence analysis showed that pyruvate decarboxylase (one of the most abundant proteins in Zymomonas mobilis) contains 559 amino acids. The promoter for the gene encoding pyruvate decarboxylase was not recognized by Escherichia coli, although the cloned gene was expressed at relatively high levels under the control of alternative promoters. The promoter
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8. Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli.
Pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis purified to homogeneity by using dye-ligand and ion-exchange chromatography. Antibodies produced against the enzyme and the amino-terminal sequence obtained for the pure enzyme were used to select and confirm the identity of a genomic clone encoding the enzyme selected from a genomic library of Z. mo
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9. Nucleotide sequence of the pyruvate decarboxylase gene from Zymomonas mobilis.
Pyruvate decarboxylase (EC 4.1.1.1), the penultimate enzyme in the alcoholic fermentation pathway of Zymomonas mobilis, converts pyruvate to acetaldehyde and carbon dioxide. The complete nucleotide sequence of the structural gene encoding pyruvate decarboxylase from Zymomonas mobilis has been determined. The coding region is 1704 nucleotides long and encodes
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10. Pyruvate Decarboxylase Catalyzes Decarboxylation of Branched-Chain 2-Oxo Acids but Is Not Essential for Fusel Alcohol Production by Saccharomyces cerevisiae
The fusel alcohols 3-methyl-1-butanol, 2-methyl-1-butanol, and 2-methyl-propanol are important flavor compounds in yeast-derived food products and beverages. The formation of these compounds from branched-chain amino acids is generally assumed to occur via the Ehrlich pathway, which involves the concerted action of a branched-chain transaminase, a decarboxyl
American Society for Microbiology.
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11. Effect of hexoses on the levels of pyruvate decarboxylase in Mucor rouxii.
Pyruvate decarboxylase activity in the dimorphic fungus Mucor rouxii increased 25- to 35-fold in yeastlike and mycelial cells grown in the presence of glucose as compared to the activity observed in mycelial cultures grown in the absence of glucose.
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12. Metabolic responses of pyruvate decarboxylase-negative Saccharomyces cerevisiae to glucose excess.
In Saccharomyces cerevisiae, oxidation of pyruvate to acetyl coenzyme A can occur via two routes. In pyruvate decarboxylase-negative (Pdc-) mutants, the pyruvate dehydrogenase complex is the sole functional link between glycolysis and the tricarboxylic acid (TCA) cycle. Such mutants therefore provide a useful experimental system with which to study regulatio