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Relevant bibliographies by topics / Pyruvate decarboxylase

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Academic literature on the topic 'Pyruvate decarboxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Pyruvate decarboxylase"

1

Pegg, Anthony E. "S-Adenosylmethionine decarboxylase." Essays in Biochemistry 46 (October 30, 2009): 25–46. http://dx.doi.org/10.1042/bse0460003.

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S-Adenosylmethionine decarboxylase is a key enzyme for the synthesis of polyamines in mammals, plants and many other species that use aminopropyltransferases for this pathway. It catalyses the formation of S-adenosyl-1-(methylthio)-3-propylamine (decarboxylated S-adenosylmethionine), which is used as the aminopropyl donor. This is the sole function of decarboxylated S-adenosylmethionine. Its content is therefore kept very low and is regulated by variation in the activity of S-adenosylmethionine decarboxylase according to the need for polyamine synthesis. All S-adenosylmethionine decarboxylases

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2

ter Schure, Eelko G., Marcel T. Flikweert, Johannes P. van Dijken, Jack T. Pronk, and C. Theo Verrips. "Pyruvate Decarboxylase Catalyzes Decarboxylation of Branched-Chain 2-Oxo Acids but Is Not Essential for Fusel Alcohol Production by Saccharomyces cerevisiae." Applied and Environmental Microbiology 64, no. 4 (1998): 1303–7. http://dx.doi.org/10.1128/aem.64.4.1303-1307.1998.

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ABSTRACT 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 decarboxylase, and an alcohol dehydrogenase. Partially purified preparations of pyruvate decarboxylase (EC 4.1.1.1 ) have been reported to catalyze the decarboxylation of the branched-chain 2-oxo acids formed upon transamination of leucine,

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3

Tylicki, Adam, Jan Czerniecki, Pawel Dobrzyn, Agnieszka Matanowska, Anna Olechno, and Slawomir Strumilo. "Modification of thiamine pyrophosphate dependent enzyme activity by oxythiamine in Saccharomyces cerevisiae cells." Canadian Journal of Microbiology 51, no. 10 (2005): 833–39. http://dx.doi.org/10.1139/w05-072.

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Oxythiamine is an antivitamin derivative of thiamine that after phosphorylation to oxythiamine pyro phos phate can bind to the active centres of thiamine-dependent enzymes. In the present study, the effect of oxythiamine on the viability of Saccharomyces cerevisiae and the activity of thiamine pyrophosphate dependent enzymes in yeast cells has been investigated. We observed a decrease in pyruvate decarboxylase specific activity on both a control and an oxythiamine medium after the first 6 h of culture. The cytosolic enzymes transketolase and pyruvate decarboxylase decreased their specific acti

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4

Janati-Idrissi, Rachid, Anne-Marie Junelles, Abdellah El Kanouni, Henri Petitdemange, and Robert Gay. "Pyruvate fermentation by Clostridium acetobutylicum." Biochemistry and Cell Biology 67, no. 10 (1989): 735–39. http://dx.doi.org/10.1139/o89-110.

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Clostridium acetobutylicum ATCC 824 using pyruvate as the sole carbon source produced mainly acetate and butyrate as end products of fermentation. Acetate and butyrate kinase activities were higher in cells growing in the presence of pyruvate than glucose, whereas the level of the acetoacetate decarboxylase, an enzyme involved in solvent formation, was lower. Similar activities of glyceraldehyde-3-phosphate dehydrogenase were found in cells grown in pyruvate and glucose mediums. The transfer of C. acetobutylicum from pyruvate to glucose medium suggested that pyruvate represses the "solventogen

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5

Romagnoli, Gabriele, Marijke A. H. Luttik, Peter Kötter, Jack T. Pronk, and Jean-Marc Daran. "Substrate Specificity of Thiamine Pyrophosphate-Dependent 2-Oxo-Acid Decarboxylases in Saccharomyces cerevisiae." Applied and Environmental Microbiology 78, no. 21 (2012): 7538–48. http://dx.doi.org/10.1128/aem.01675-12.

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ABSTRACTFusel alcohols are precursors and contributors to flavor and aroma compounds in fermented beverages, and some are under investigation as biofuels. The decarboxylation of 2-oxo acids is a key step in the Ehrlich pathway for fusel alcohol production. InSaccharomyces cerevisiae, five genes share sequence similarity with genes encoding thiamine pyrophosphate-dependent 2-oxo-acid decarboxylases (2ODCs).PDC1,PDC5, andPDC6encode differentially regulated pyruvate decarboxylase isoenzymes;ARO10encodes a 2-oxo-acid decarboxylase with broad substrate specificity, andTHI3has not yet been shown to

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6

Atsumi, Shota, Zhen Li, and James C. Liao. "Acetolactate Synthase from Bacillus subtilis Serves as a 2-Ketoisovalerate Decarboxylase for Isobutanol Biosynthesis in Escherichia coli." Applied and Environmental Microbiology 75, no. 19 (2009): 6306–11. http://dx.doi.org/10.1128/aem.01160-09.

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ABSTRACTA pathway toward isobutanol production previously constructed inEscherichia coliinvolves 2-ketoacid decarboxylase (Kdc) fromLactococcus lactisthat decarboxylates 2-ketoisovalerate (KIV) to isobutyraldehyde. Here, we showed that a strain lacking Kdc is still capable of producing isobutanol. We found that acetolactate synthase fromBacillus subtilis(AlsS), which originally catalyzes the condensation of two molecules of pyruvate to form 2-acetolactate, is able to catalyze the decarboxylation of KIV like Kdc both in vivo and in vitro. Mutational studies revealed that the replacement of Q487

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7

Xun, Zhao, Rogers Peter L., Eilhann E. Kwon, Sang Chul Jeong, and Young Jae Jeon. "Growth Characteristics of a Pyruvate Decarboxylase Mutant Strain of Zymomonas mobilis." Journal of Life Science 25, no. 11 (2015): 1290–97. http://dx.doi.org/10.5352/jls.2015.25.11.1290.

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8

Krieger, Florian, Michael Spinka, Ralph Golbik, Gerhard Hübner, and Stephan König. "Pyruvate decarboxylase from Kluyveromyces lactis." European Journal of Biochemistry 269, no. 13 (2002): 3256–63. http://dx.doi.org/10.1046/j.1432-1033.2002.03006.x.

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Eram, Mohammad S., Erica Oduaran, and Kesen Ma. "The Bifunctional Pyruvate Decarboxylase/Pyruvate Ferredoxin Oxidoreductase fromThermococcus guaymasensis." Archaea 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/349379.

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The hyperthermophilic archaeonThermococcus guaymasensisproduces ethanol as a metabolic end product, and an alcohol dehydrogenase (ADH) catalyzing the reduction of acetaldehyde to ethanol has been purified and characterized. However, the enzyme catalyzing the formation of acetaldehyde has not been identified. In this study an enzyme catalyzing the production of acetaldehyde from pyruvate was purified and characterized fromT. guaymasensisunder strictly anaerobic conditions. The enzyme had both pyruvate decarboxylase (PDC) and pyruvate ferredoxin oxidoreductase (POR) activities. It was oxygen sen

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10

Spaepen, Stijn, Wim Versées, Dörte Gocke, Martina Pohl, Jan Steyaert, and Jos Vanderleyden. "Characterization of Phenylpyruvate Decarboxylase, Involved in Auxin Production of Azospirillum brasilense." Journal of Bacteriology 189, no. 21 (2007): 7626–33. http://dx.doi.org/10.1128/jb.00830-07.

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ABSTRACT Azospirillum brasilense belongs to the plant growth-promoting rhizobacteria with direct growth promotion through the production of the phytohormone indole-3-acetic acid (IAA). A key gene in the production of IAA, annotated as indole-3-pyruvate decarboxylase (ipdC), has been isolated from A. brasilense, and its regulation was reported previously (A. Vande Broek, P. Gysegom, O. Ona, N. Hendrickx, E. Prinsen, J. Van Impe, and J. Vanderleyden, Mol. Plant-Microbe Interact. 18:311-323, 2005). An ipdC-knockout mutant was found to produce only 10% (wt/vol) of the wild-type IAA production leve

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Dissertations / Theses on the topic "Pyruvate decarboxylase"

1

Blalock, LeeAnn Talarico. "Expression of pyruvate decarboxylase in a Gram positive host Sarcina ventriculi pyruvate decarboxylase versus other known pyruvate decarboxylases /." [Gainesville, Fla.] : University of Florida, 2003. http://purl.fcla.edu/fcla/etd/UFE0002366.

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2

Cheung, Wing Yee. "A yeast pyruvate decarboxylase regulatory gene." Thesis, Imperial College London, 1985. http://hdl.handle.net/10044/1/37659.

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Brown, Audrey Elaine. "Constructing a recombinant model of the human pyruvate dehydrogenase complex." Thesis, University of Glasgow, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.248119.

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4

Rose, Janet Elizabeth. "Mechanistic studies on glutamate decarboxylase and serine hydroxmethyltransferase." Thesis, University of St Andrews, 1993. http://hdl.handle.net/10023/14295.

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(2S)- and (2R)-Serine O-sulphate have been synthesised and shown to inactivate glutamate decarboxylase (GAD) from E. Coli. Novel methodology was developed to enable the stereospecific synthesis of (2S) and (2R)-deuteriated serine in order to probe the mechanism of inactivation. The rates of inactivation of glutamate decarboxylase by (2S)-, (2S)-[2-2H]-, (2R)- and (2R)-[2-2H]-serine O-sulphate have been measured for each of the isotopomers at a range of concentrations. From the data obtained the deuterium isotope effects were determined for each enantiomer. The inactivation by the (2S)-enantiom

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5

Green, J. B. A. "Control of pyruvate decarboxylase and phospho-glucose isomerase in yeast." Thesis, Imperial College London, 1988. http://hdl.handle.net/10044/1/47087.

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6

Buddrus, Lisa. "Creation and evaluation of a pyruvate decarboxylase dependent ethanol fermentation pathway in Geobacillus thermoglucosidasius." Thesis, University of Bath, 2017. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.715253.

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Bioethanol, produced from organic waste as a second-generation biofuel, is an important renewable energy source. Here, recalcitrant carbohydrate sources, such as municipal and agricultural waste, and plants grown on land not suitable for food crops, are exploited. The thermophilic, Gram-positive bacterium Geobacillus thermoglucosidasius is naturally very flexible in its growth substrates and produces a variety of fermentation products, including lactate, formate, acetate and ethanol. TMO Renewables Ltd. used metabolic engineering to enhance ethanol production, creating the production strain TM

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Alcover, Fortuny Natàlia. "Asymmetric synthesis of chiral amines using transaminases: a multienzymatic approach by pyruvate decarboxylase coupling." Doctoral thesis, Universitat Autònoma de Barcelona, 2021. http://hdl.handle.net/10803/671815.

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La present tesi es centra en el desenvolupament i optimització d’una estratègia basada en la biocatàlisi per a la síntesi d’amines quirals, les quals són compostos òpticament actius de gran valor que poden ésser utilitzats per a la síntesi de nombrosos productes, especialment en les indústries farmacèutica i agroquímica. Més concretament, es pretén sintetitzar 3-amino-1-fenilbutà (3-APB) i 1-feniletilamina (1-PEA) a través de la reacció en cascada de la transaminasa (TA) i la piruvat decarboxilasa (PDC). Aquesta cascada es basa en una síntesi asimètrica que parteix de les seves corresponents c

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Bornemann, Stephen. "Studies on pyruvate decarboxylase-catalysed acyloin formation and the effects of surfactants on lipase-catalysed hydrolysis of esters." Thesis, University of Warwick, 1992. http://wrap.warwick.ac.uk/110304/.

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The effect of surfactants on the hydrolysis of achiral and chiral substrates by crude and purified porcine pancreatic lipase (PPL; EC 3.1.1.3) has been studied. Rather than accelerating the reactions, surfactants slowed down ("inhibited") the reactions relative to the rate in the absence of surfactant, despite effective emulsification of the substrate. Surfactants varied in the extent to which the reaction was inhibited and inhibition occurred below the critical micelle concentration of surfactants. Inhibition was accompanied by a loss of enantioselectivity with the crude enzyme but not the pu

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Leksawasdi, Noppol Biotechnology &amp Biomolecular Sciences (BABS) UNSW. "Kinetics and modelling of enzymatic process for R-phenylacetylcarbinol (PAC) production." Awarded by:University of New South Wales. Biotechnology and Biomolecular Sciences (BABS), 2004. http://handle.unsw.edu.au/1959.4/20846.

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R-phenylacetylcarbinol (PAC) is used as a precursor for production of ephedrine and pseudoephedrine, which are anti-asthmatics and nasal decongestants. PAC is produced from benzaldehyde and pyruvate mediated by pyruvate decarboxylase (PDC). A strain of Rhizopus javanicus was evaluated for its production of PDC. The morphology of R. javanicus was influenced by the degree of aeration/agitation. A relatively high specific PDC activity (328 U decarboxylase g-1 mycelium) was achieved when aeration/agitation were reduced significantly in the latter stages of cultivation. The stability of partially

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10

Acar, Seyda. "Biochemical And Genetic Studies On The Pyruvate Branch Point Enzymes Of Rhizopus Oryzae." Phd thesis, METU, 2004. http://etd.lib.metu.edu.tr/upload/3/12604762/index.pdf.

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Rhizopus oryzae is a filamentous fungi which produces lactic acid and ethanol in fermentations. R. oryzae has numerous advantages for use industrial production of L-(+)-lactic acid but the yield of lactic acid produced on the basis of carbon consumed is low. Metabolic flux analysis of R. oryzae has shown that most of the pyruvate produced at the end of the glycolysis is channelled to ethanol, acetyl-CoA and oxaloacetate production. This study aimed to answer some questions addressed on the regulation of pyruvate branch point in R. oryzae and for this purpose biochemical characterisation of the

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Books on the topic "Pyruvate decarboxylase"

1

Bornemann, Stephen. Studies on pyruvate decarboxylase-catalysed acyloin formation and the effects of surfactants on lipase-catalysedhydrolysis of esters. typescript, 1992.

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2

Gish, Gerald Daniel. A mechanistic investigation of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase. 1986.

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Book chapters on the topic "Pyruvate decarboxylase"

1

Schomburg, Dietmar, and Margit Salzmann. "Pyruvate decarboxylase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_1.

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Schomburg, Dietmar, and Margit Salzmann. "2, 2-Dialkylglycine decarboxylase (pyruvate)." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_60.

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3

Maskevich, A. A., and I. P. Chernikevich. "Study of Fluorescence Decay of Pyruvate Decarboxylase." In Fifth International Conference on the Spectroscopy of Biological Molecules. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1934-4_141.

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4

Pohl, Martina. "Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis." In New Enzymes for Organic Synthesis. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/bfb0103301.

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5

Hohmann, Stefan. "Pyruvate Decarboxylases." In Yeast Sugar Metabolism. CRC Press, 2024. http://dx.doi.org/10.1201/9781003578987-11.

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6

Jordan, Frank, Min Liu, Eduard Sergienko, et al. "Yeast Pyruvate Decarboxylase." In Thiamine. CRC Press, 2003. http://dx.doi.org/10.1201/9780203913420.ch12.

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7

Hodgson, J. A., N. A. Woodward, L. Welsh, M. Moir, and J. D. Brown. "Fermentation studies with pyruvate decarboxylase mutants of Saccharomyces cerevisiae." In European Brewery Convention. Oxford University PressOxford, 1993. http://dx.doi.org/10.1093/oso/9780199634668.003.0051.

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Abstract Acetate esters of higher alcohols formed during fermentation of worts by Saccharomyces cerevisiae have an important influence on beer character and flavour. The availability of specific higher alcohols for metabolic esterification is a factor controlling the levels of isopentyl acetate and isobutyl acetate formed. Fermentation and growth studies were performed on genetic constructs of yeast which have been deleted for the genes encoding pyruvate decarboxylase. This allowed the direct demonstration of a specific branched-chain oxo-acid decarboxylase responsible for higher alcohol synth

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8

Siegert, Petra, Martina Pohl, Malea Kneen, Irina Pogozheva, George Kenyon, and Michael McLeish. "Exploring the Substrate Specificity of Benzoylformate Decarboxylase, Pyruvate Decarboxylase, and Benzaldehyde Lyase." In Thiamine. CRC Press, 2003. http://dx.doi.org/10.1201/9780203913420.ch16.

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9

Frey, Perry A., and Adrian D. Hegeman. "Decarboxylation and Carboxylation." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0012.

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Decarboxylation is an essential process in catabolic metabolism of essentially all nutrients that serve as sources of energy in biological cells and organisms. The most widely known biological process leading to decarboxylation is the metabolism of glucose, in which all of the carbon in the molecule is oxidized to carbon dioxide by way of the glycolytic pathway, the pyruvate dehydrogenase complex, and the tricarboxylic acid cycle. The decarboxylation steps take place in thiamine pyrophosphate (TPP)–dependent α-ketoacid dehydrogenase complexes and isocitrate dehydrogenase. The latter enzyme doe

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DOWHAM, W., and Q. X. LI. "Mechanism of Formation of the Pyruvate Prosthetic Group of Phosphatidylserine Decarboxylase of Escherichia Coli." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50092-3.

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Conference papers on the topic "Pyruvate decarboxylase"

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Maskevich, Sergei A., Ivan P. Chernikevich, Gennedy A. Gachko, Leonid N. Kivach, and Nataliya D. Strekal. "Study of pyruvate decarboxylase and thiamine kinase from brewer's yeast by SERS." In Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, edited by Jouko E. Korppi-Tommola. SPIE, 1993. http://dx.doi.org/10.1117/12.146134.

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Reports on the topic "Pyruvate decarboxylase"

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Thongchul, Nuttha. Development of itaconic acid production technology for bioplastic using immobilized Aspergillus terreus on natural fiber in the static bed bioreactor. Chulalongkorn University, 2015. https://doi.org/10.58837/chula.res.2015.99.

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Aspergillus terreus was reported as the promising fungal strain for itaconic acid; however, the commercial production suffers from the low yield. Low production yield was claimed as the result of completing TCA cycle towards biomass synthesis while under limiting phosphate and nitrogen, TCA cycle was somewhat shunted and consequently the metabolite fluxes move towards itaconic acid production route. By regulating enzymes in TCA cycle, it is believed that itaconic acid production can be improved. One of the key responsible enzymes involved in itaconic acid production was triggered in this study

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2

Or, Etti, David Galbraith, and Anne Fennell. Exploring mechanisms involved in grape bud dormancy: Large-scale analysis of expression reprogramming following controlled dormancy induction and dormancy release. United States Department of Agriculture, 2002. http://dx.doi.org/10.32747/2002.7587232.bard.

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The timing of dormancy induction and release is very important to the economic production of table grape. Advances in manipulation of dormancy induction and dormancy release are dependent on the establishment of a comprehensive understanding of biological mechanisms involved in bud dormancy. To gain insight into these mechanisms we initiated the research that had two main objectives: A. Analyzing the expression profiles of large subsets of genes, following controlled dormancy induction and dormancy release, and assessing the role of known metabolic pathways, known regulatory genes and novel se

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3

(Pyruvate decarboxylase: A key enzyme for alcohol production). Office of Scientific and Technical Information (OSTI), 1989. http://dx.doi.org/10.2172/5454091.

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