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Journal articles on the topic 'Pyruvate decarboxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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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

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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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9

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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11

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 (1994): 207–10. http://dx.doi.org/10.1111/j.1574-6968.1994.tb06766.x.

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12

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

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13

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

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14

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 (2005): 91–99. http://dx.doi.org/10.1016/j.jbiotec.2004.08.002.

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15

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

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16

Zhong, Wenhe, Hugh P. Morgan, Matthew W. Nowicki, et al. "Pyruvate kinases have an intrinsic and conserved decarboxylase activity." Biochemical Journal 458, no. 2 (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

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 (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 invol

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18

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 (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 (

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19

Macêdo, Larissa Félix, Franciscleudo Bezerra da Costa, Ana Marinho do Nascimento, et al. "Pyruvate decarboxylase in minimally processed young palm cladode." Research, Society and Development 9, no. 7 (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 F

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20

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 (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 Kl

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21

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 (1999): 73–79. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13551.x.

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22

Thomas, G., R. Diefenbach, and R. G. Duggleby. "Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate." Biochemical Journal 266, no. 1 (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 becau

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23

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 (2003): 315–20. http://dx.doi.org/10.1080/10242420310001630164.

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24

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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25

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

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26

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

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27

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

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28

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 (1996): 761–70. http://dx.doi.org/10.1007/bf00019464.

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29

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

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30

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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31

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 (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

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32

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 (1993): 99–102. http://dx.doi.org/10.1016/0014-5793(93)80973-x.

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33

Bartasun, Paulina, Nicole Prandi, Marko Storch, et al. "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 Synechocy

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34

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 (1996): 1867–73. http://dx.doi.org/10.1021/ja951830t.

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35

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 (1999): 173–77. http://dx.doi.org/10.1016/s1389-1723(99)80197-2.

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36

Velmurugan, Soundarapandian, Zita Lobo, and Pabitra K. Maitra. "Suppression of pdc2 Regulating Pyruvate Decarboxylase Synthesis in Yeast." Genetics 145, no. 3 (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 th

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37

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 (2008): 1359–65. http://dx.doi.org/10.1007/s10529-008-9698-1.

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38

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

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39

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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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 (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 ter

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41

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

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42

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 (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 dec

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43

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 (2015): 347–50. http://dx.doi.org/10.1080/21655979.2015.1112472.

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44

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 (1990): 3222–23. http://dx.doi.org/10.1021/ja00164a059.

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45

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 (2016): 190. http://dx.doi.org/10.3390/catal6120190.

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46

Li, Tong, Pierre Juteau, Réjean Beaudet, François Lépine, Richard Villemur, and Jean-Guy Bisaillon. "Purification and characterization of a 4-hydroxybenzoate decarboxylase from an anaerobic coculture." Canadian Journal of Microbiology 46, no. 9 (2000): 856–59. http://dx.doi.org/10.1139/w00-067.

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The oxygen-sensitive 4-hydroxybenzoate decarboxylase (4OHB-DC) activity from a phenol-carboxylating coculture, consisting of Clostridium-like strain 6 and an unidentified strain 7, was studied. Assays done with cell extracts showed that the optimal pH was 5.0-6.5 and the Kmwas 5.4 mM. The activity decreased by 50% in the presence of 5 mM EDTA, and it was restored and even enhanced by the addition of Mg++, Mn++, Zn++, or Ca++. After purification, the molecular mass of the enzyme was estimated as 420 kDa by gel chromatography, and as 119 kDa by SDS-PAGE, suggesting a homotetrameric structure. It

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

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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 (2006): 4199–209. http://dx.doi.org/10.1111/j.1742-4658.2006.05415.x.

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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 (1998): 20196–204. http://dx.doi.org/10.1074/jbc.273.32.20196.

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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 (1991): 2811–15. http://dx.doi.org/10.1099/00221287-137-12-2811.

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