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Journal articles on the topic 'Pyruvate decarboxylase'

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Published: 4 June 2021

Last updated: 29 January 2023

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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 have a covalently bound pyruvate prosthetic group, which is essential for the decarboxylation reaction, and have similar structures, although they differ with respect to activation by cations, primary sequence and subunit composition. The present chapter describes these features, the mechanisms for autocatalytic generation of the pyruvate from a proenzyme precursor and for the decarboxylation reaction, and the available inhibitors of this enzyme, which have uses as anticancer and anti-trypanosomal agents. The intricate mechanisms for regulation of mammalian S-adenosylmethionine decarboxylase activity and content are also described.

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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 (April 1, 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, isoleucine, and valine. Indeed, in a coupled enzymatic assay with horse liver alcohol dehydrogenase, cell extracts of a wild-type Saccharomyces cerevisiae strain exhibited significant decarboxylation rates with these branched-chain 2-oxo acids. Decarboxylation of branched-chain 2-oxo acids was not detectable in cell extracts of an isogenic strain in which all threePDC genes had been disrupted. Experiments with cell extracts from S. cerevisiae mutants expressing a singlePDC gene demonstrated that both PDC1- andPDC5-encoded isoenzymes can decarboxylate branched-chain 2-oxo acids. To investigate whether pyruvate decarboxylase is essential for fusel alcohol production by whole cells, wild-type S. cerevisiae and an isogenic pyruvate decarboxylase-negative strain were grown on ethanol with a mixture of leucine, isoleucine, and valine as the nitrogen source. Surprisingly, the three corresponding fusel alcohols were produced in both strains. This result proves that decarboxylation of branched-chain 2-oxo acids via pyruvate decarboxylase is not an essential step in fusel alcohol production.

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3

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 (November 30, 2015): 1290–97. http://dx.doi.org/10.5352/jls.2015.25.11.1290.

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4

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

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5

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 (September 1, 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 activity in the presence of oxythiamine but only during the beginning of the cultivation. However, after 12 h of cultivation, oxythiamine-treated cells showed higher specific activity of cytosolic enzymes. More over, it was established by SDS–PAGE that the high specific activity of pyruvate decarboxylase was followed by an increase in the amount of the enzyme protein. In contrast, the mitochondrial enzymes, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes, were inhibited by oxythiamine during the entire experiment. Our results suggest that the observed strong decrease in growth rate and viability of yeast on medium with oxythiamine may be due to stronger in hibition of mitochondrial pyruvate dehydrogenase than of cytosolic enzymes.Key words: pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase, transketolase, pyruvate decarboxylase, activity, oxythiamine, inhibition.

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6

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 (October 1, 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 "solventogenesis."Key words: Clostridium acetobutylicum, pyruvic acid, kinase, acetoacetate decarboxylase.

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7

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 (August 17, 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 encode an active decarboxylase. Despite the importance of fusel alcohol production inS. cerevisiae, the substrate specificities of these five 2ODCs have not been systematically compared. When the five 2ODCs were individually overexpressed in apdc1Δpdc5Δpdc6Δaro10Δthi3Δ strain, only Pdc1, Pdc5, and Pdc6 catalyzed the decarboxylation of the linear-chain 2-oxo acids pyruvate, 2-oxo-butanoate, and 2-oxo-pentanoate in cell extracts. The presence of a Pdc isoenzyme was also required for the production ofn-propanol andn-butanol in cultures grown on threonine and norvaline, respectively, as nitrogen sources. These results demonstrate the importance of pyruvate decarboxylases in the natural production ofn-propanol andn-butanol byS. cerevisiae. No decarboxylation activity was found for Thi3 with any of the substrates tested. Only Aro10 and Pdc5 catalyzed the decarboxylation of the aromatic substrate phenylpyruvate, with Aro10 showing superior kinetic properties. Aro10, Pdc1, Pdc5, and Pdc6 exhibited activity with all branched-chain and sulfur-containing 2-oxo acids tested but with markedly different decarboxylation kinetics. The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols.

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8

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 sensitive, and the optimal temperatures were 85°C and >95°C for the PDC and POR activities, respectively. The purified enzyme had activities of3.8±0.22 U mg−1and20.2±1.8 U mg−1, with optimal pH-values of 9.5 and 8.4 for each activity, respectively. Coenzyme A was essential for both activities, although it did not serve as a substrate for the former. Enzyme kinetic parameters were determined separately for each activity. The purified enzyme was a heterotetramer. The sequences of the genes encoding the subunits of the bifunctional PDC/POR were determined. It is predicted that all hyperthermophilicβ-keto acids ferredoxin oxidoreductases are bifunctional, catalyzing the activities of nonoxidative and oxidative decarboxylation of the correspondingβ-keto acids.

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9

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 (August 14, 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 with amino acids with small side chains (Ala, Ser, and Gly) diminished only the decarboxylase activity but maintained the synthase activity.

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10

Sanchis, Vicente, Inmaculada Vinas, Ian N. Roberts, David J. Jeenes, Adrian J. Watson, and David B. Archer. "A pyruvate decarboxylase gene fromAspergillus parasiticus." FEMS Microbiology Letters 117, no. 2 (April 1994): 207–10. http://dx.doi.org/10.1111/j.1574-6968.1994.tb06766.x.

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11

Lee, Thomas C., and Pat J. Langston-Unkefer. "Pyruvate Decarboxylase from Zea mays L." Plant Physiology 79, no. 1 (September 1, 1985): 242–47. http://dx.doi.org/10.1104/pp.79.1.242.

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12

Langston-Unkefer, Pat J., and Thomas C. Lee. "Pyruvate Decarboxylase from Zea mays L." Plant Physiology 79, no. 2 (October 1, 1985): 436–40. http://dx.doi.org/10.1104/pp.79.2.436.

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13

Rosche, Bettina, Michael Breuer, Bernhard Hauer, and Peter L. Rogers. "Role of pyruvate in enhancing pyruvate decarboxylase stability towards benzaldehyde." Journal of Biotechnology 115, no. 1 (January 2005): 91–99. http://dx.doi.org/10.1016/j.jbiotec.2004.08.002.

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14

Lindqvist, Ylva, and Gunter Schneider. "Thiamin diphosphate dependent enzymes: transketolase, pyruvate oxidase and pyruvate decarboxylase." Current Opinion in Structural Biology 3, no. 6 (January 1993): 896–901. http://dx.doi.org/10.1016/0959-440x(93)90153-c.

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15

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 (August 31, 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 level. In this study, the encoded enzyme is characterized via a biochemical and phylogenetic analysis. Therefore, the recombinant enzyme was expressed and purified via heterologous overexpression in Escherichia coli and subsequent affinity chromatography. The molecular mass of the holoenzyme was determined by size-exclusion chromatography, suggesting a tetrameric structure, which is typical for 2-keto acid decarboxylases. The enzyme shows the highest k cat value for phenylpyruvate. Comparing values for the specificity constant k cat/Km , indole-3-pyruvate is converted 10-fold less efficiently, while no activity could be detected with benzoylformate. The enzyme shows pronounced substrate activation with indole-3-pyruvate and some other aromatic substrates, while for phenylpyruvate it appears to obey classical Michaelis-Menten kinetics. Based on these data, we propose a reclassification of the ipdC gene product of A. brasilense as a phenylpyruvate decarboxylase (EC 4.1.1.43).

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16

Zhong, Wenhe, Hugh P. Morgan, Matthew W. Nowicki, Iain W. McNae, Meng Yuan, Juraj Bella, Paul A. M. Michels, Linda A. Fothergill-Gilmore, and Malcolm D. Walkinshaw. "Pyruvate kinases have an intrinsic and conserved decarboxylase activity." Biochemical Journal 458, no. 2 (February 14, 2014): 301–11. http://dx.doi.org/10.1042/bj20130790.

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We provide an enzyme mechanism for the decarboxylase activity of pyruvate kinase which is conserved from protozoa to mammals. Structural and solution studies of range of related dicarboxylic acids suggest the decarboxylase activity is restricted to oxaloacetate as a substrate.

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17

Buddrus, Lisa, Emma S. V. Andrews, David J. Leak, Michael J. Danson, Vickery L. Arcus, and Susan J. Crennell. "Crystal structure of pyruvate decarboxylase fromZymobacter palmae." Acta Crystallographica Section F Structural Biology Communications 72, no. 9 (August 26, 2016): 700–706. http://dx.doi.org/10.1107/s2053230x16012012.

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Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg2+ion-dependent enzyme that catalyses the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. It is rare in bacteria, but is a key enzyme in homofermentative metabolism, where ethanol is the major product. Here, the previously unreported crystal structure of the bacterial pyruvate decarboxylase fromZymobacter palmaeis presented. The crystals were shown to diffract to 2.15 Å resolution. They belonged to space groupP21, with unit-cell parametersa= 204.56,b= 177.39,c= 244.55 Å andRr.i.m.= 0.175 (0.714 in the highest resolution bin). The structure was solved by molecular replacement using PDB entry 2vbi as a model and the finalRvalues wereRwork= 0.186 (0.271 in the highest resolution bin) andRfree= 0.220 (0.300 in the highest resolution bin). Each of the six tetramers is a dimer of dimers, with each monomer sharing its thiamine pyrophosphate across the dimer interface, and some contain ethylene glycol mimicking the substrate pyruvate in the active site. Comparison with other bacterial PDCs shows a correlation of higher thermostability with greater tetramer interface area and number of interactions.

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18

Zimmer, Wolfgang, Barbara Hundeshagen, and Edith Niederau. "Demonstration of the indolepyruvate decarboxylase gene homologue in different auxin-producing species of the Enterobacteriaceae." Canadian Journal of Microbiology 40, no. 12 (December 1, 1994): 1072–76. http://dx.doi.org/10.1139/m94-170.

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Different Enterobacteriaceae were assayed for their ability to produce the plant hormone indole-3-acetate with the aim to study the distribution of the indole-3-pyruvate pathway, which is known to be involved in the production of indole-3-acetate in a root-associated Enterobacter cloacae strain. Other E. cloacae strains, and also Enterobacter agglomerans strains, Pantoea agglomerans, Klebsiella aerogenes, and Klebsiella oxytoca were found to convert tryptophan into indole-3-acetate. As it was also intended to identify the conserved regions of the indole-3-pyruvate decarboxylase, which is involved in producing indole-3-acetate in the E. cloacae strain, oligonucleotide primers were synthesized for different regions of the corresponding gene. One pair of these primers allowed us to amplify a segment of the predicted size by the polymerase chain reaction with DNA of the seven different Enterobacteriaceae that produce indole-3-acetate. Segments of five strains were cloned and sequenced. All sequences showed significant homology to the indole-3-pyruvate decarboxylase gene. As in addition a positive DNA–DNA hybridization signal was detected in the seven strains using the E. cloacae or E. agglomerans segments as a probe, indole-3-acetate biosynthesis is suggested to be catalyzed via the indole-3-pyruvate pathway not only in E. cloacae but also in the other soil-living Enterobacteriaceae. Conserved regions were detected in the indole-3-decarboxylase by alignment of the now-available five different partial sequences. These regions should enable identification of the gene in other bacterial families or even in plants.Key words: indole-3-pyruvate decarboxylase, indole-3-acetic acid production, auxin, polymerase chain reaction, Enterobacteriaceae.

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19

Macêdo, Larissa Félix, Franciscleudo Bezerra da Costa, Ana Marinho do Nascimento, Jéssica Leite da Silva, Osvaldo Soares da Silva, Charlene Maria Alcântara, Tatiana Marinho Gadelha, Álvaro Gustavo Ferreira da Silva, Giuliana Naiara Barros Sales, and Pahlevi Augusto de Souza. "Pyruvate decarboxylase in minimally processed young palm cladode." Research, Society and Development 9, no. 7 (May 16, 2020): e340973755. http://dx.doi.org/10.33448/rsd-v9i7.3755.

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The palm is a cactaceous of great global importance, being the young cladodes minimally processed a viable alternative consumption for cooking. Among the studied palm variables, enzymes play a major role in the post-harvest quality of these species, generating oxidation and influencing the sensory attributes of cladodes. Therefore, the objective was to estimate the pyruvate decarboxylase activity in young cladodes of 'Tiny' palms - Nopalea cochenilifera and 'Ear Mexican Elephant' - Opuntia tuna minimally processed. The experiment was conducted in the Laboratory of Chemistry, Biochemistry and Food Analysis Center of Science and Technology Agrifood the Federal University of Campina Grande, Campus Pombal, Paraíba. The young cladodes were minimally processed and the analyzes were performed immediately after processing, with 24 and 48 hours of incubation under controlled temperature (22 ± 2°C). The analyzes performed were activity of the enzyme pyruvate decarboxylase (PDC), pH, soluble solids, titratable acidity, ratio, soluble sugars, total chlorophyll, total carotenoids, ascorbic acid and phenolic compounds. There was enzymatic activity of pyruvate decarboxylase from young minimally processed cladodes for the species studied, with greater activity in the cladodes of the species 'Tiny'.

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20

Flikweert, Marcel T., Martin Swaaf, Johannes P. Dijken, and Jack T. Pronk. "Growth requirements of pyruvate-decarboxylase-negativeSaccharomyces cerevisiae." FEMS Microbiology Letters 174, no. 1 (May 1999): 73–79. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13551.x.

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21

Thomas, G., R. Diefenbach, and R. G. Duggleby. "Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate." Biochemical Journal 266, no. 1 (February 15, 1990): 305–8. http://dx.doi.org/10.1042/bj2660305.

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Pyruvate decarboxylase from Zymomonas mobilis is inhibited by 3-hydroxypyruvate, which can also act as a poor substrate. While catalysing the decarboxylation of this alternative substrate, the enzyme undergoes a progressive but partial inactivation over several hours. The extent of inactivation depends upon the pH and upon the concentration of 3-hydroxypyruvate. After partial inactivation and removal of unchanged 3-hydroxypyruvate, enzymic activity recovers slowly. We suggest that inactivation results from accumulation of enzyme-bound glycollaldehyde, which is relatively stable, possibly because it is dehydrated to form an acetyl group.

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22

Leksawasdi, Noppol, Michael Breuer, Bernhard Hauer, Bettina Rosche, and Peter L. Rogers. "Kinetics of Pyruvate Decarboxylase Deactivation by Benzaldehyde." Biocatalysis and Biotransformation 21, no. 6 (December 2003): 315–20. http://dx.doi.org/10.1080/10242420310001630164.

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23

Peguin, Sophie, Pierre R. Coulet, and Gilbert Bardeletti. "Pyruvate oxidase and oxaloacetate decarboxylase enzyme electrodes." Analytica Chimica Acta 222, no. 1 (1989): 83–93. http://dx.doi.org/10.1016/s0003-2670(00)81882-6.

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24

Lockington, Robin A., Glenn N. Borlace, and Joan M. Kelly. "Pyruvate decarboxylase and anaerobic survival in Aspergillusnidulans." Gene 191, no. 1 (May 1997): 61–67. http://dx.doi.org/10.1016/s0378-1119(97)00032-2.

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25

Kelley, Philip M. "Maize pyruvate decarboxylase mRNA is induced anaerobically." Plant Molecular Biology 13, no. 2 (August 1989): 213–22. http://dx.doi.org/10.1007/bf00016139.

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26

Hossain, M. Anwar, Enamul Huq, Anil Grover, Elizabeth S. Dennis, W. James Peacock, and Thomas K. Hodges. "Characterization of pyruvate decarboxylase genes from rice." Plant Molecular Biology 31, no. 4 (July 1996): 761–70. http://dx.doi.org/10.1007/bf00019464.

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27

Skory, Christopher D. "Induction of Rhizopus oryzae Pyruvate Decarboxylase Genes." Current Microbiology 47, no. 1 (July 1, 2003): 59–64. http://dx.doi.org/10.1007/s00284-002-3933-0.

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28

Kelley, Philip M., Kris Godfrey, Shailesh K. Lal, and Mary Alleman. "Characterization of the maize pyruvate decarboxylase gene." Plant Molecular Biology 17, no. 6 (December 1991): 1259–61. http://dx.doi.org/10.1007/bf00028743.

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29

Robinson, Brian H., and Kathy Chun. "The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex." FEBS Letters 328, no. 1-2 (August 9, 1993): 99–102. http://dx.doi.org/10.1016/0014-5793(93)80973-x.

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30

Bianchi, Michele M., Luca Brambilla, Francesca Protani, Chi-Li Liu, Jefferson Lievense, and Danilo Porro. "Efficient Homolactic Fermentation byKluyveromyces lactis Strains Defective in Pyruvate Utilization and Transformed with the HeterologousLDH Gene." Applied and Environmental Microbiology 67, no. 12 (December 1, 2001): 5621–25. http://dx.doi.org/10.1128/aem.67.12.5621-5625.2001.

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ABSTRACT A high yield of lactic acid per gram of glucose consumed and the absence of additional metabolites in the fermentation broth are two important goals of lactic acid production by microrganisms. Both purposes have been previously approached by using aKluyveromyces lactis yeast strain lacking the single pyruvate decarboxylase gene (KlPDC1) and transformed with the heterologous lactate dehydrogenase gene (LDH). The LDH gene was placed under the control theKlPDC1 promoter, which has allowed very high levels of lactate dehydrogenase (LDH) activity, due to the absence of autoregulation by KlPdc1p. The maximal yield obtained was 0.58 g g−1, suggesting that a large fraction of the glucose consumed was not converted into pyruvate. In a different attempt to redirect pyruvate flux toward homolactic fermentation, we usedK. lactis LDH transformant strains deleted of the pyruvate dehydrogenase (PDH) E1α subunit gene. A great process improvement was obtained by the use of producing strains lacking both PDH and pyruvate decarboxylase activities, which showed yield levels of as high as 0.85 g g−1 (maximum theoretical yield, 1 g g−1), and with high LDH activity.

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31

Lobell, Mario, and David H. G. Crout. "Pyruvate Decarboxylase: A Molecular Modeling Study of Pyruvate Decarboxylation and Acyloin Formation." Journal of the American Chemical Society 118, no. 8 (January 1996): 1867–73. http://dx.doi.org/10.1021/ja951830t.

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32

Miyata, Reiko, and Tetsu Yonehara. "Breeding of high-pyruvate-producing Torulopsis glabrata with acquired reduced pyruvate decarboxylase." Journal of Bioscience and Bioengineering 88, no. 2 (January 1999): 173–77. http://dx.doi.org/10.1016/s1389-1723(99)80197-2.

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33

Sutiono, Samuel, Katharina Satzinger, André Pick, Jörg Carsten, and Volker Sieber. "To beat the heat – engineering of the most thermostable pyruvate decarboxylase to date." RSC Advances 9, no. 51 (2019): 29743–46. http://dx.doi.org/10.1039/c9ra06251c.

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34

Tsai, C. S., J. L. Shi, B. W. Beehler, and B. Beck. "Enzyme activities of D-glucose metabolism in the fission yeast Schizosaccharomyces pombe." Canadian Journal of Microbiology 38, no. 12 (December 1, 1992): 1313–19. http://dx.doi.org/10.1139/m92-216.

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The activities of key enzymes that are members of D-glucose metabolic pathways in Schizosaccharomyces pombe undergoing respirative, respirofermentative, and fermentative metabolisms are monitored. The steady-state activities of glycolytic enzymes, except phosphofructokinase, decrease with a reduced efficiency in D-glucose utilization by yeast continuous culture. On the other hand, the enzymic activities of pentose monophosphate pathway reach the maximum when the cell mass production of the cultures is optimum. Enzymes of tricarboxylate cycle exhibit the maximum activities at approximately the washout rate. The steady-state activity of pyruvate dehydrogenase complex increases rapidly when D-glucose is efficiently utilized. By comparison, the activity of pyruvate decarboxylase begins to increase only when ethanol production occurs. Depletion of dissolved oxygen suppresses the activity of pyruvate dehydrogenase complex but facilitates that of pyruvate decarboxylase. Acetate greatly enhances the acetyl CoA synthetase activity. Similarly, ethanol stimulates alcohol dehydrogenase and aldehyde dehydrogenase activities. Evidence for the existence of alcohol dehydrogenase isozymes in the fission yeast is presented. Key words: yeast, glucose-metabolizing enzymes.

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35

Thompson, Ann H., David J. Studholme, Edward M. Green, and David J. Leak. "Heterologous expression of pyruvate decarboxylase in Geobacillus thermoglucosidasius." Biotechnology Letters 30, no. 8 (March 27, 2008): 1359–65. http://dx.doi.org/10.1007/s10529-008-9698-1.

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Chen, Allen Kuan-Liang, Michael Breuer, Bernhard Hauer, Peter L. Rogers, and Bettina Rosche. "pH shift enhancement ofCandida utilis pyruvate decarboxylase production." Biotechnology and Bioengineering 92, no. 2 (2005): 183–88. http://dx.doi.org/10.1002/bit.20588.

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37

Nixon, Peter F., Russell J. Diefenbach, and Ronald G. Duggleby. "Inhibition of transketolase and pyruvate decarboxylase by omeprazole." Biochemical Pharmacology 44, no. 1 (July 1992): 177–79. http://dx.doi.org/10.1016/0006-2952(92)90053-l.

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38

Bartasun, Paulina, Nicole Prandi, Marko Storch, Yarin Aknin, Mark Bennett, Arianna Palma, Geoff Baldwin, Yumiko Sakuragi, Patrik R. Jones, and John Rowland. "The effect of modulating the quantity of enzymes in a model ethanol pathway on metabolic flux in Synechocystis sp. PCC 6803." PeerJ 7 (August 28, 2019): e7529. http://dx.doi.org/10.7717/peerj.7529.

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Synthetic metabolism allows new metabolic capabilities to be introduced into strains for biotechnology applications. Such engineered metabolic pathways are unlikely to function optimally as initially designed and native metabolism may not efficiently support the introduced pathway without further intervention. To develop our understanding of optimal metabolic engineering strategies, a two-enzyme ethanol pathway consisting of pyruvate decarboxylase and acetaldehyde reductase was introduced into Synechocystis sp. PCC 6803. We characteriseda new set of ribosome binding site sequences in Synechocystis sp. PCC 6803 providing a range of translation strengths for different genes under test. The effect of ribosome-bindingsite sequence, operon design and modifications to native metabolism on pathway flux was analysed by HPLC. The accumulation of all introduced proteins was also quantified using selected reaction monitoring mass spectrometry. Pathway productivity was more strongly dependent on the accumulation of pyruvate decarboxylase than acetaldehyde reductase. In fact, abolishment of reductase over-expression resulted in the greatest ethanol productivity, most likely because strains harbouringsingle-gene constructs accumulated more pyruvate decarboxylase than strains carrying any of the multi-gene constructs. Overall, several lessons were learned. Firstly, the expression level of the first gene in anyoperon influenced the expression level of subsequent genes, demonstrating that translational coupling can also occur in cyanobacteria. Longer operons resulted in lower protein abundance for proximally-encoded cistrons. And, implementation of metabolic engineering strategies that have previously been shown to enhance the growth or yield of pyruvate dependent products, through co-expression with pyruvate kinase and/or fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase, indicated that other factors had greater control over growth and metabolic flux under the tested conditions.

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39

Yoshida, Shiori, Hideki Tanaka, Makoto Hirayama, Kousaku Murata, and Shigeyuki Kawai. "Production of pyruvate from mannitol by mannitol-assimilating pyruvate decarboxylase-negative Saccharomyces cerevisiae." Bioengineered 6, no. 6 (November 2, 2015): 347–50. http://dx.doi.org/10.1080/21655979.2015.1112472.

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40

Annan, Nikoi, and Frank Jordan. "Flavo pyruvate decarboxylase: a semisynthetic enzyme model for pyruvate oxidase and acetolactate synthetase." Journal of the American Chemical Society 112, no. 8 (April 1990): 3222–23. http://dx.doi.org/10.1021/ja00164a059.

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Velmurugan, Soundarapandian, Zita Lobo, and Pabitra K. Maitra. "Suppression of pdc2 Regulating Pyruvate Decarboxylase Synthesis in Yeast." Genetics 145, no. 3 (March 1, 1997): 587–94. http://dx.doi.org/10.1093/genetics/145.3.587.

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Mutants lacking pyruvate decarboxylase cannot grow on glucose. We have isolated three different complementation groups of extragenic suppressors that suppress mutations in pdc2, a regulatory locus required for the synthesis of the glycolytic enzyme pyruvate decarboxylase. The most frequent of these is a recessive mutation in the structural gene PFK1 of the soluble phosphofructokinase. The other class XSP18 (extragenic suppressor of pdc2) is a dominant temperature-sensitive suppressor that allows the cells to grow on glucose only at 30° but not at 36°. It also affects the normal induction of the glucose-inducible enolase 2, which can be rescued by providing a copy of wild-type xsp18 in trans-heterozygotes. The pyruvate decarboxylase activity in the triple mutant pdc2 pfk1 XSP18 is nearly equal to the sum of the activities in the two double mutants pdc2 pfk1 and pdc2 XSP18, respectively. This implies that the two suppressors act through independent pathways or that there is no cooperativity between them. In the pdc2 pfk1 XSP18 strain, pfk1 suppresses the loss of induction of glucose-inducible enolase 2 brought about by XSP18, but fails to rescue temperature sensitivity. The third class (xsp37) supports the growth of the pdc2 mutant on glucose but fails to support growth on gluconeogenic carbon sources. All the three suppressors suppress pdc2Δ as well and act on PDC1 at the level of transcription.

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42

Kaczowka, Steven J., Christopher J. Reuter, Lee A. Talarico, and Julie A. Maupin-Furlow. "Recombinant production ofZymomonas mobilispyruvate decarboxylase in the haloarchaeonHaloferax volcanii." Archaea 1, no. 5 (2005): 327–34. http://dx.doi.org/10.1155/2005/325738.

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The unusual physiological properties of archaea (e.g., growth in extreme salt concentration, temperature and pH) make them ideal platforms for metabolic engineering. Towards the ultimate goal of modifying an archaeon to produce bioethanol or other useful products, the pyruvate decarboxylase gene ofZymomonas mobilis(Zmpdc) was expressed inHaloferax volcanii. This gene has been used successfully to channel pyruvate to ethanol in various Gram-negative bacteria, includingEscherichia coli. Although the ionic strength of theH. volcaniicytosol differs over 15-fold from that ofE. coli, gel filtration and circular dichroism revealed no difference in secondary structure between the ZmPDC protein isolated from either of these hosts. Like theE. colipurified enzyme, ZmPDC fromH. volcaniicatalyzed the nonoxidative decarboxylation of pyruvate. A decrease in the amount of soluble ZmPDC protein was detected asH. volcaniitransitioned from log phase to late stationary phase that was inversely proportional to the amount ofpdc-specific mRNA. Based on these results, proteins from non-halophilic organisms can be actively synthesized in haloarchaea; however, post-transcriptional mechanisms present in stationary phase appear to limit the amount of recombinant protein expressed.

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Andrews, Forest, Cindy Wechsler, Megan Rogers, Danilo Meyer, Kai Tittmann, and Michael McLeish. "Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity." Catalysts 6, no. 12 (November 30, 2016): 190. http://dx.doi.org/10.3390/catal6120190.

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Christopher, Mary E., and Allen G. Good. "Evolution of a functionally related lactate dehydrogenase and pyruvate decarboxylase pseudogene complex in maize." Genome 42, no. 6 (December 1, 1999): 1167–75. http://dx.doi.org/10.1139/g99-094.

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A large proportion of the maize genome is repetitive DNA (60-80%) with retrotransposons contributing significantly to the repetitive DNA component. The majority of retrotransposon DNA is located in intergenic regions and is organized in a nested fashion. Analysis of an 8.2-kb segment of maize genomic DNA demonstrated the presence of three retrotransposons of different reiteration classes in addition to lactate dehydrogenase and pyruvate decarboxylase pseudogenes. Both of the pseudogenes were located within a defective retrotransposon element (LP-like element) which possessed identical long terminal repeats (LTRs) with inverted repeats at each end, a primer binding site, a polypurine tract, and generated a 5-bp target site duplication. A model describing the events leading to the formation of the LP-like element is proposed.Key words: lactate dehydrogenase, LP-like element, pseudogene, pyruvate decarboxylase, retrotransposon.

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Vuralhan, Zeynep, Marcos A. Morais, Siew-Leng Tai, Matthew D. W. Piper, and Jack T. Pronk. "Identification and Characterization of Phenylpyruvate Decarboxylase Genes in Saccharomyces cerevisiae." Applied and Environmental Microbiology 69, no. 8 (August 2003): 4534–41. http://dx.doi.org/10.1128/aem.69.8.4534-4541.2003.

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ABSTRACT Catabolism of amino acids via the Ehrlich pathway involves transamination to the corresponding α-keto acids, followed by decarboxylation to an aldehyde and then reduction to an alcohol. Alternatively, the aldehyde may be oxidized to an acid. This pathway is functional in Saccharomyces cerevisiae, since during growth in glucose-limited chemostat cultures with phenylalanine as the sole nitrogen source, phenylethanol and phenylacetate were produced in quantities that accounted for all of the phenylalanine consumed. Our objective was to identify the structural gene(s) required for the decarboxylation of phenylpyruvate to phenylacetaldehyde, the first specific step in the Ehrlich pathway. S. cerevisiae possesses five candidate genes with sequence similarity to genes encoding thiamine diphosphate-dependent decarboxylases that could encode this activity: YDR380w/ARO10, YDL080C/THI3, PDC1, PDC5, and PDC6. Phenylpyruvate decarboxylase activity was present in cultures grown with phenylalanine as the sole nitrogen source but was absent from ammonia-grown cultures. Furthermore, the transcript level of one candidate gene (ARO10) increased 30-fold when phenylalanine replaced ammonia as the sole nitrogen source. Analyses of phenylalanine catabolite production and phenylpyruvate decarboxylase enzyme assays indicated that ARO10 was sufficient to encode phenylpyruvate decarboxylase activity in the absence of the four other candidate genes. There was also an alternative activity with a higher capacity but lower affinity for phenylpyruvate. The candidate gene THI3 did not itself encode an active phenylpyruvate decarboxylase but was required along with one or more pyruvate decarboxylase genes (PDC1, PDC5, and PDC6) for the alternative activity. The Km and V max values of the two activities differed, showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells. Modifications to this gene could therefore be important for metabolic engineering of the Ehrlich pathway.

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46

Kuo, D. J., G. Dikdan, and F. Jordan. "Resolution of brewers' yeast pyruvate decarboxylase into two isozymes." Journal of Biological Chemistry 261, no. 7 (March 1986): 3316–19. http://dx.doi.org/10.1016/s0021-9258(17)35784-8.

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47

Kutter, Steffen, Georg Wille, Sandy Relle, Manfred S. Weiss, Gerhard Hubner, and Stephan Konig. "The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis." FEBS Journal 273, no. 18 (September 2006): 4199–209. http://dx.doi.org/10.1111/j.1742-4658.2006.05415.x.

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48

Dobritzsch, Doreen, Stephan König, Gunter Schneider, and Guoguang Lu. "High Resolution Crystal Structure of Pyruvate Decarboxylase fromZymomonas mobilis." Journal of Biological Chemistry 273, no. 32 (August 7, 1998): 20196–204. http://dx.doi.org/10.1074/jbc.273.32.20196.

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49

Candy, J. M., R. G. Duggleby, and J. S. Mattick. "Expression of active yeast pyruvate decarboxylase in Escherichia coli." Journal of General Microbiology 137, no. 12 (December 1, 1991): 2811–15. http://dx.doi.org/10.1099/00221287-137-12-2811.

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50

Buddrus, Lisa, Emma S. V. Andrews, David J. Leak, Michael J. Danson, Vickery L. Arcus, and Susan J. Crennell. "Crystal structure of an inferred ancestral bacterial pyruvate decarboxylase." Acta Crystallographica Section F Structural Biology Communications 74, no. 3 (February 26, 2018): 179–86. http://dx.doi.org/10.1107/s2053230x18002819.

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Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a key enzyme in homofermentative metabolism where ethanol is the major product. PDCs are thiamine pyrophosphate- and Mg2+ion-dependent enzymes that catalyse the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. As this enzyme class is rare in bacteria, current knowledge of bacterial PDCs is extremely limited. One approach to further the understanding of bacterial PDCs is to exploit the diversity provided by evolution. Ancestral sequence reconstruction (ASR) is a method of computational molecular evolution to infer extinct ancestral protein sequences, which can then be synthesized and experimentally characterized. Through ASR a novel PDC was generated, designated ANC27, that shares only 78% amino-acid sequence identity with its closest extant homologue (Komagataeibacter medellinensisPDC, GenBank accession No. WP_014105323.1), yet is fully functional. Crystals of this PDC diffracted to 3.5 Å resolution. The data were merged in space groupP3221, with unit-cell parametersa=b =108.33,c= 322.65 Å, and contained two dimers (two tetramer halves) in the asymmetric unit. The structure was solved by molecular replacement using PDB entry 2wvg as a model, and the finalRvalues wereRwork= 0.246 (0.3671 in the highest resolution bin) andRfree= 0.319 (0.4482 in the highest resolution bin). Comparison with extant bacterial PDCs supports the previously observed correlation between decreased tetramer interface area (and number of interactions) and decreased thermostability.

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