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Journal articles on the topic 'Entner-Doudoroff'

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Published: 9 March 2023

Last updated: 10 March 2023

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1

Mendz, G. L., S. L. Hazell, and B. P. Burns. "The Entner-Doudoroff Pathway in Helicobacter pylori." Archives of Biochemistry and Biophysics 312, no. 2 (August 1994): 349–56. http://dx.doi.org/10.1006/abbi.1994.1319.

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2

Peekhaus, N., and T. Conway. "What’s for Dinner?: Entner-Doudoroff Metabolism inEscherichia coli." Journal of Bacteriology 180, no. 14 (July 15, 1998): 3495–502. http://dx.doi.org/10.1128/jb.180.14.3495-3502.1998.

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3

Held, Gary, and Manuel Goldman. "Pathways of glucose catabolism in the smut fungus Ustilago violacea." Canadian Journal of Microbiology 32, no. 1 (January 1, 1986): 56–61. http://dx.doi.org/10.1139/m86-011.

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The pathways of glucose catabolism were examined in haploid and diploid strains of the smut fungus Ustilago violacea. Radiorespirometric studies indicated that both of the haploid mating types and diploid strains of this basidiomycete catabolized glucose through the Embden–Meyerhof and hexose monophosphate shunt pathways. The Entner–Doudoroff pathway was not utilized by any of the strains examined. Radiorespirometric data also suggested functioning of an active tricarboxylic acid cycle. In vitro enzyme assays established the presence in this organism of all the enzymes integral to the operative pathways plus the presence of the enzymes of the glyoxylate cycle. Enzyme activities specific to the Entner–Doudoroff pathway were not detected. No major differences in the routes of glucose dissimilation were found between the two haploid mating types or between haploid and diploid forms of this organism.

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4

Conway, Tyrrell. "The Entner-Doudoroff pathway: history, physiology and molecular biology." FEMS Microbiology Letters 103, no. 1 (September 1992): 1–28. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05822.x.

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5

Hager, Paul W., M. Worth Calfee, and Paul V. Phibbs. "The Pseudomonas aeruginosa devB/SOL Homolog,pgl, Is a Member of the hex Regulon and Encodes 6-Phosphogluconolactonase." Journal of Bacteriology 182, no. 14 (July 15, 2000): 3934–41. http://dx.doi.org/10.1128/jb.182.14.3934-3941.2000.

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ABSTRACT A cyclic version of the Entner-Doudoroff pathway is used byPseudomonas aeruginosa to metabolize carbohydrates. Genes encoding the enzymes that catabolize intracellular glucose to pyruvate and glyceraldehyde 3-phosphate are coordinately regulated, clustered at 39 min on the chromosome, and collectively form thehex regulon. Within the hex cluster is an open reading frame (ORF) with homology to the devB/SOLfamily of unidentified proteins. This ORF encodes a protein of either 243 or 238 amino acids; it overlaps the 5′ end of zwf (encodes glucose-6-phosphate dehydrogenase) and is followed immediately by eda (encodes the Entner-Doudoroff aldolase). The devB/SOL homolog was inactivated in P. aeruginosa PAO1 by recombination with a suicide plasmid containing an interrupted copy of the gene, creating mutant strain PAO8029. PAO8029 grows at 9% of the wild-type rate using mannitol as the carbon source and at 50% of the wild-type rate using gluconate as the carbon source. Cell extracts of PAO8029 were specifically deficient in 6-phosphogluconolactonase (Pgl) activity. The cloned devB/SOL homolog complemented PAO8029 to restore normal growth on mannitol and gluconate and restored Pgl activity. Hence, we have identified this gene as pgland propose that the devB/SOL family members encode 6-phosphogluconolactonases. Interestingly, three eukaryotic glucose-6-phosphate dehydrogenase (G6PDH) isozymes, from human, rabbit, and Plasmodium falciparum, contain Pgl domains, suggesting that the sequential reactions of G6PDH and Pgl are incorporated in a single protein. 6-Phosphogluconolactonase activity is induced in P. aeruginosa PAO1 by growth on mannitol and repressed by growth on succinate, and it is expressed constitutively in P. aeruginosa PAO8026 (hexR). Taken together, these results establish that Pgl is an essential enzyme of the cyclic Entner-Doudoroff pathway encoded by pgl, a structural gene of the hex regulon.

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6

Lamble, Henry J., Christine C. Milburn, Garry L. Taylor, David W. Hough, and Michael J. Danson. "Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway inSulfolobus solfataricus." FEBS Letters 576, no. 1-2 (September 15, 2004): 133–36. http://dx.doi.org/10.1016/j.febslet.2004.08.074.

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7

Felux, Ann-Katrin, Dieter Spiteller, Janosch Klebensberger, and David Schleheck. "Entner–Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1." Proceedings of the National Academy of Sciences 112, no. 31 (July 20, 2015): E4298—E4305. http://dx.doi.org/10.1073/pnas.1507049112.

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Sulfoquinovose (SQ; 6-deoxy-6-sulfoglucose) is the polar head group of the plant sulfolipid SQ-diacylglycerol, and SQ comprises a major proportion of the organosulfur in nature, where it is degraded by bacteria. A first degradation pathway for SQ has been demonstrated recently, a “sulfoglycolytic” pathway, in addition to the classical glycolytic (Embden–Meyerhof) pathway in Escherichia coli K-12; half of the carbon of SQ is abstracted as dihydroxyacetonephosphate (DHAP) and used for growth, whereas a C3-organosulfonate, 2,3-dihydroxypropane sulfonate (DHPS), is excreted. The environmental isolate Pseudomonas putida SQ1 is also able to use SQ for growth, and excretes a different C3-organosulfonate, 3-sulfolactate (SL). In this study, we revealed the catabolic pathway for SQ in P. putida SQ1 through differential proteomics and transcriptional analyses, by in vitro reconstitution of the complete pathway by five heterologously produced enzymes, and by identification of all four organosulfonate intermediates. The pathway follows a reaction sequence analogous to the Entner–Doudoroff pathway for glucose-6-phosphate: It involves an NAD+-dependent SQ dehydrogenase, 6-deoxy-6-sulfogluconolactone (SGL) lactonase, 6-deoxy-6-sulfogluconate (SG) dehydratase, and 2-keto-3,6-dideoxy-6-sulfogluconate (KDSG) aldolase. The aldolase reaction yields pyruvate, which supports growth of P. putida, and 3-sulfolactaldehyde (SLA), which is oxidized to SL by an NAD(P)+-dependent SLA dehydrogenase. All five enzymes are encoded in a single gene cluster that includes, for example, genes for transport and regulation. Homologous gene clusters were found in genomes of other P. putida strains, in other gamma-Proteobacteria, and in beta- and alpha-Proteobacteria, for example, in genomes of Enterobacteria, Vibrio, and Halomonas species, and in typical soil bacteria, such as Burkholderia, Herbaspirillum, and Rhizobium.

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8

Sutter, Jan-Moritz, Julia-Beate Tästensen, Ulrike Johnsen, Jörg Soppa, and Peter Schönheit. "Key Enzymes of the Semiphosphorylative Entner-Doudoroff Pathway in the Haloarchaeon Haloferax volcanii: Characterization of Glucose Dehydrogenase, Gluconate Dehydratase, and 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase." Journal of Bacteriology 198, no. 16 (June 13, 2016): 2251–62. http://dx.doi.org/10.1128/jb.00286-16.

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ABSTRACTThe halophilic archaeonHaloferax volcaniihas been proposed to degrade glucose via the semiphosphorylative Entner-Doudoroff (spED) pathway. So far, the key enzymes of this pathway, glucose dehydrogenase (GDH), gluconate dehydratase (GAD), and 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase (KDPGA), have not been characterized, and their functional involvement in glucose degradation has not been demonstrated. Here we report that the genes HVO_1083 and HVO_0950 encode GDH and KDPGA, respectively. The recombinant enzymes show high specificity for glucose and KDPG and did not convert the corresponding C4epimers galactose and 2-keto-3-deoxy-6-phosphogalactonate at significant rates. Growth studies of knockout mutants indicate the functional involvement of both GDH and KDPGA in glucose degradation. GAD was purified fromH. volcanii, and the encoding gene,gad, was identified as HVO_1488. GAD catalyzed the specific dehydration of gluconate and did not utilize galactonate at significant rates. A knockout mutant of GAD lost the ability to grow on glucose, indicating the essential involvement of GAD in glucose degradation. However, following a prolonged incubation period, growth of the Δgadmutant on glucose was recovered. Evidence is presented that under these conditions, GAD was functionally replaced by xylonate dehydratase (XAD), which uses both xylonate and gluconate as substrates. Together, the characterization of key enzymes and analyses of the respective knockout mutants present conclusive evidence for thein vivooperation of the spED pathway for glucose degradation inH. volcanii.IMPORTANCEThe work presented here describes the identification and characterization of the key enzymes glucose dehydrogenase, gluconate dehydratase, and 2-keto-3-deoxy-6-phosphogluconate aldolase and their encoding genes of the proposed semiphosphorylative Entner-Doudoroff pathway in the haloarchaeonHaloferax volcanii. The functional involvement of the three enzymes was proven by analyses of the corresponding knockout mutants. These results provide evidence for thein vivooperation of the semiphosphorylative Entner-Doudoroff pathway in haloarchaea and thus expand our understanding of the unusual sugar degradation pathways in the domainArchaea.

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9

Ahmed, H., B. Tjaden, R. Hensel, and B. Siebers. "Embden–Meyerhof–Parnas and Entner–Doudoroff pathways in Thermoproteus tenax: metabolic parallelism or specific adaptation?" Biochemical Society Transactions 32, no. 2 (April 1, 2004): 303–4. http://dx.doi.org/10.1042/bst0320303.

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Genome data as well as biochemical studies have indicated that – as a peculiarity within hyperthermophilic Archaea – Thermoproteus tenax uses three different pathways for glucose metabolism, a variant of the reversible EMP (Embden–Meyerhof–Parnas) pathway and two different modifications of the ED (Entner–Doudoroff) pathway, a non-phosphorylative and a semi-phosphorylative version. An overview of the three different pathways is presented and the physiological function of the variants is discussed.

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10

Kresge, Nicole, Robert D. Simoni, and Robert L. Hill. "The Entner-Doudoroff Pathway for Glucose Degradation: the Work of MichaelDoudoroff." Journal of Biological Chemistry 280, no. 27 (July 2005): e24-e25. http://dx.doi.org/10.1016/s0021-9258(20)61415-6.

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11

Ponce, Elizabeth, Mauricio García, and Ma Enriqueta Muñoz. "Participation of the Entner–Doudoroff pathway inEscherichia colistrains with an inactive phosphotransferase system (PTS–Glc+) in gluconate and glucose batch cultures." Canadian Journal of Microbiology 51, no. 11 (November 1, 2005): 975–82. http://dx.doi.org/10.1139/w05-101.

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The activity of the enzymes of the central metabolic pathways has been the subject of intensive analysis; however, the Entner–Doudoroff (ED) pathway has only recently begun to attract attention. The metabolic response to edd gene knockout in Escherichia coli JM101 and PTS–Glc+was investigated in gluconate and glucose batch cultures and compared with other pyruvate kinase and PTS mutants previously constructed. Even though the specific growth rates between the strain carrying the edd gene knockout and its parent JM101 and PTS–Glc+edd and its parent PTS–Glc+were very similar, reproducible changes in the specific consumption rates and biomass yields were obtained when grown on glucose. These results support the participation of the ED pathway not only on gluconate metabolism but on other metabolic and biochemical processes in E. coli. Despite that gluconate is a non-PTS carbohydrate, the PTS–Glc+and derived strains showed important reductions in the specific growth and gluconate consumption rates. Moreover, the overall activity of the ED pathway on gluconate resulted in important increments in PTS–Glc+and PTS-Glc+pykF mutants. Additional results obtained with the pykA pykF mutant indicate the important contribution of the pyruvate kinase enzymes to pyruvate synthesis and energy production in both carbon sources.Key words: Escherichia coli, gluconate metabolism, Entner-Doudoroff pathway, PT system, pyruvate kinase isoenzymes.

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12

del Castillo, Teresa, Estrella Duque, and Juan L. Ramos. "A Set of Activators and Repressors Control Peripheral Glucose Pathways in Pseudomonas putida To Yield a Common Central Intermediate." Journal of Bacteriology 190, no. 7 (February 1, 2008): 2331–39. http://dx.doi.org/10.1128/jb.01726-07.

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ABSTRACT Pseudomonas putida KT2440 channels glucose to the central Entner-Doudoroff intermediate 6-phosphogluconate through three convergent pathways. The genes for these convergent pathways are clustered in three independent regions on the host chromosome. A number of monocistronic units and operons coexist within each of these clusters, favoring coexpression of catabolic enzymes and transport systems. Expression of the three pathways is mediated by three transcriptional repressors, HexR, GnuR, and PtxS, and by a positive transcriptional regulator, GltR-2. In this study, we generated mutants in each of the regulators and carried out transcriptional assays using microarrays and transcriptional fusions. These studies revealed that HexR controls the genes that encode glucokinase/glucose 6-phosphate dehydrogenase that yield 6-phosphogluconate; the genes for the Entner-Doudoroff enzymes that yield glyceraldehyde-3-phosphate and pyruvate; and gap-1, which encodes glyceraldehyde-3-phosphate dehydrogenase. GltR-2 is the transcriptional regulator that controls specific porins for the entry of glucose into the periplasmic space, as well as the gtsABCD operon for glucose transport through the inner membrane. GnuR is the repressor of gluconate transport and gluconokinase responsible for the conversion of gluconate into 6-phosphogluconate. PtxS, however, controls the enzymes for oxidation of gluconate to 2-ketogluconate, its transport and metabolism, and a set of genes unrelated to glucose metabolism.

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13

Holten, Eirik. "6-PHOSPHOGLUCONATE DEHYDROGENASE AND ENZYMES OF THE ENTNER-DOUDOROFF PATHWAY IN NEISSERIA." Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology 82B, no. 2 (August 15, 2009): 207–13. http://dx.doi.org/10.1111/j.1699-0463.1974.tb02313.x.

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14

Gunnarsson, Nina, Uffe H. Mortensen, Margherita Sosio, and Jens Nielsen. "Identification of the Entner-Doudoroff pathway in an antibiotic-producing actinomycete species." Molecular Microbiology 52, no. 3 (April 1, 2004): 895–902. http://dx.doi.org/10.1111/j.1365-2958.2004.04028.x.

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15

Figueiredo, Ana Sofia, Theresa Kouril, Dominik Esser, Patrick Haferkamp, Patricia Wieloch, Dietmar Schomburg, Peter Ruoff, Bettina Siebers, and Jörg Schaber. "Systems biology of the modified branched Entner-Doudoroff pathway in Sulfolobus solfataricus." PLOS ONE 12, no. 7 (July 10, 2017): e0180331. http://dx.doi.org/10.1371/journal.pone.0180331.

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16

Okano, Kenji, Qianqin Zhu, and Kohsuke Honda. "In vitro reconstitution of non-phosphorylative Entner–Doudoroff pathway for lactate production." Journal of Bioscience and Bioengineering 129, no. 3 (March 2020): 269–75. http://dx.doi.org/10.1016/j.jbiosc.2019.09.010.

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17

Ahmed, Hatim, Thijs J. G. Ettema, Britta Tjaden, Ans C. M. Geerling, John van der Oost, and Bettina Siebers. "The semi-phosphorylative Entner–Doudoroff pathway in hyperthermophilic archaea: a re-evaluation." Biochemical Journal 390, no. 2 (August 23, 2005): 529–40. http://dx.doi.org/10.1042/bj20041711.

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Biochemical studies have suggested that, in hyperthermophilic archaea, the metabolic conversion of glucose via the ED (Entner–Doudoroff) pathway generally proceeds via a non-phosphorylative variant. A key enzyme of the non-phosphorylating ED pathway of Sulfolobus solfataricus, KDG (2-keto-3-deoxygluconate) aldolase, has been cloned and characterized previously. In the present study, a comparative genomics analysis is described that reveals conserved ED gene clusters in both Thermoproteus tenax and S. solfataricus. The corresponding ED proteins from both archaea have been expressed in Escherichia coli and their specificity has been identified, revealing: (i) a novel type of gluconate dehydratase (gad gene), (ii) a bifunctional 2-keto-3-deoxy-(6-phospho)-gluconate aldolase (kdgA gene), (iii) a 2-keto-3-deoxygluconate kinase (kdgK gene) and, in S. solfataricus, (iv) a GAPN (non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; gapN gene). Extensive in vivo and in vitro enzymatic analyses indicate the operation of both the semi-phosphorylative and the non-phosphorylative ED pathway in T. tenax and S. solfataricus. The existence of this branched ED pathway is yet another example of the versatility and flexibility of the central carbohydrate metabolic pathways in the archaeal domain.

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18

Lamble, Henry J., Alex Theodossis, Christine C. Milburn, Garry L. Taylor, Steven D. Bull, David W. Hough, and Michael J. Danson. "Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeonSulfolobus solfataricus." FEBS Letters 579, no. 30 (December 1, 2005): 6865–69. http://dx.doi.org/10.1016/j.febslet.2005.11.028.

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19

Waligora, E. A., C. R. Fisher, N. J. Hanovice, A. Rodou, E. E. Wyckoff, and S. M. Payne. "Role of Intracellular Carbon Metabolism Pathways in Shigella flexneri Virulence." Infection and Immunity 82, no. 7 (April 14, 2014): 2746–55. http://dx.doi.org/10.1128/iai.01575-13.

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ABSTRACTShigella flexneri, which replicates in the cytoplasm of intestinal epithelial cells, can use the Embden-Meyerhof-Parnas, Entner-Doudoroff, or pentose phosphate pathway for glycolytic carbon metabolism. To determine which of these pathways is used by intracellularS. flexneri, mutants were constructed and tested in a plaque assay for the ability to invade, replicate intracellularly, and spread to adjacent epithelial cells. Mutants blocked in the Embden-Meyerhof-Parnas pathway (pfkABandpykAFmutants) invaded the cells but formed very small plaques. Loss of the Entner-Doudoroff pathway geneedaresulted in small plaques, but the doubleeda eddmutant formed normal-size plaques. This suggested that the plaque defect of theedamutant was due to buildup of the toxic intermediate 2-keto-3-deoxy-6-phosphogluconic acid rather than a specific requirement for this pathway. Loss of the pentose phosphate pathway had no effect on plaque formation, indicating that it is not critical for intracellularS. flexneri. Supplementation of the epithelial cell culture medium with pyruvate allowed the glycolysis mutants to form larger plaques than those observed with unsupplemented medium, consistent with data from phenotypic microarrays (Biolog) indicating that pyruvate metabolism was not disrupted in these mutants. Interestingly, the wild-typeS. flexnerialso formed larger plaques in the presence of supplemental pyruvate or glucose, with pyruvate yielding the largest plaques. Analysis of the metabolites in the cultured cells showed increased intracellular levels of the added compound. Pyruvate increased the growth rate ofS. flexneriin vitro, suggesting that it may be a preferred carbon source inside host cells.

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20

Maleki, Susan, Mali Mærk, Svein Valla, and Helga Ertesvåg. "Mutational Analyses of Glucose Dehydrogenase and Glucose-6-Phosphate Dehydrogenase Genes in Pseudomonas fluorescens Reveal Their Effects on Growth and Alginate Production." Applied and Environmental Microbiology 81, no. 10 (March 6, 2015): 3349–56. http://dx.doi.org/10.1128/aem.03653-14.

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ABSTRACTThe biosynthesis of alginate has been studied extensively due to the importance of this polymer in medicine and industry. Alginate is synthesized from fructose-6-phosphate and thus competes with the central carbon metabolism for this metabolite. The alginate-producing bacteriumPseudomonas fluorescensrelies on the Entner-Doudoroff and pentose phosphate pathways for glucose metabolism, and these pathways are also important for the metabolism of fructose and glycerol. In the present study, the impact of key carbohydrate metabolism enzymes on growth and alginate synthesis was investigated inP. fluorescens. Mutants defective in glucose-6-phosphate dehydrogenase isoenzymes (Zwf-1 and Zwf-2) or glucose dehydrogenase (Gcd) were evaluated using media containing glucose, fructose, or glycerol. Zwf-1 was shown to be the most important glucose-6-phosphate dehydrogenase for catabolism. Both Zwf enzymes preferred NADP as a coenzyme, although NAD was also accepted. Only Zwf-2 was active in the presence of 3 mM ATP, and then only with NADP as a coenzyme, indicating an anabolic role for this isoenzyme. Disruption ofzwf-1resulted in increased alginate production when glycerol was used as the carbon source, possibly due to decreased flux through the Entner-Doudoroff pathway rendering more fructose-6-phosphate available for alginate biosynthesis. In alginate-producing cells grown on glucose, disruption ofgcdincreased both cell numbers and alginate production levels, while this mutation had no positive effect on growth in a non-alginate-producing strain. A possible explanation is that alginate synthesis might function as a sink for surplus hexose phosphates that could otherwise be detrimental to the cell.

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21

Murray, Elizabeth L., and Tyrrell Conway. "Multiple Regulators Control Expression of the Entner-Doudoroff Aldolase (Eda) of Escherichia coli." Journal of Bacteriology 187, no. 3 (February 1, 2005): 991–1000. http://dx.doi.org/10.1128/jb.187.3.991-1000.2005.

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ABSTRACT The Escherichia coli eda gene, which encodes the Entner-Doudoroff aldolase, is central to the catabolism of several sugar acids. Here, we show that Eda synthesis is induced by growth on gluconate, glucuronate, or methyl-β-d-glucuronide; phosphate limitation; and carbon starvation. Transcription of eda initiates from three promoters, designated P1, P2, and P4, each of which is responsible for induction under different growth conditions. P1 controls eda induction on gluconate and is regulated by GntR. P2 controls eda induction on glucuronate and galacturonate and is regulated by KdgR. P4 is active under conditions of phosphate starvation and is directly controlled by PhoB. In addition, CsrA activates Eda synthesis, apparently by an indirect mechanism that may be involved in the modest changes in expression level that are associated with carbon starvation. The complex regulation of eda is discussed with respect to its several physiological roles, which apparently accommodate not only sugar acid catabolism but also detoxification of metabolites that could accumulate during starvation-induced stress.

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22

Chen, Xi, Karoline Schreiber, Jens Appel, Alexander Makowka, Berit Fähnrich, Mayo Roettger, Mohammad R. Hajirezaei, et al. "The Entner–Doudoroff pathway is an overlooked glycolytic route in cyanobacteria and plants." Proceedings of the National Academy of Sciences 113, no. 19 (April 25, 2016): 5441–46. http://dx.doi.org/10.1073/pnas.1521916113.

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Glucose degradation pathways are central for energy and carbon metabolism throughout all domains of life. They provide ATP, NAD(P)H, and biosynthetic precursors for amino acids, nucleotides, and fatty acids. It is general knowledge that cyanobacteria and plants oxidize carbohydrates via glycolysis [the Embden–Meyerhof–Parnas (EMP) pathway] and the oxidative pentose phosphate (OPP) pathway. However, we found that both possess a third, previously overlooked pathway of glucose breakdown: the Entner–Doudoroff (ED) pathway. Its key enzyme, 2-keto-3-deoxygluconate-6-phosphate (KDPG) aldolase, is widespread in cyanobacteria, moss, fern, algae, and plants and is even more common among cyanobacteria than phosphofructokinase (PFK), the key enzyme of the EMP pathway. Active KDPG aldolases from the cyanobacterium Synechocystis and the plant barley (Hordeum vulgare) were biochemically characterized in vitro. KDPG, a metabolite unique to the ED pathway, was detected in both in vivo, indicating an active ED pathway. Phylogenetic analyses revealed that photosynthetic eukaryotes acquired KDPG aldolase from the cyanobacterial ancestors of plastids via endosymbiotic gene transfer. Several Synechocystis mutants in which key enzymes of all three glucose degradation pathways were knocked out indicate that the ED pathway is physiologically significant, especially under mixotrophic conditions (light and glucose) and under autotrophic conditions in a day/night cycle, which is probably the most common condition encountered in nature. The ED pathway has lower protein costs and ATP yields than the EMP pathway, in line with the observation that oxygenic photosynthesizers are nutrient-limited, rather than ATP-limited. Furthermore, the ED pathway does not generate futile cycles in organisms that fix CO2 via the Calvin–Benson cycle.

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23

Wanken, Amy E., Tyrrell Conway, and Kathryn A. Eaton. "The Entner-Doudoroff Pathway Has Little Effect on Helicobacter pylori Colonization of Mice." Infection and Immunity 71, no. 5 (May 2003): 2920–23. http://dx.doi.org/10.1128/iai.71.5.2920-2923.2003.

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ABSTRACT Helicobacter pylori mutants deficient in 6-phosphogluconate dehydratase (6PGD) were constructed. Colonization densities were lower and minimum infectious doses were higher for mutant strains than for wild-type strains. In spite of better colonization, however, wild-type strains did not displace the mutant in cocolonization experiments. Loss of 6PGD diminishes the fitness of H. pylori in vivo, but the pathway is nonessential for colonization.

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24

Fabris, Michele, Michiel Matthijs, Stephane Rombauts, Wim Vyverman, Alain Goossens, and Gino J. E. Baart. "The metabolic blueprint of Phaeodactylum tricornutum reveals a eukaryotic Entner-Doudoroff glycolytic pathway." Plant Journal 70, no. 6 (March 31, 2012): 1004–14. http://dx.doi.org/10.1111/j.1365-313x.2012.04941.x.

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25

ISHIKAWA, Kohei, Yoshiya GUNJI, Hisashi YASUEDA, and Kozo ASANO. "Improvement ofL-Lysine Production byMethylophilus methylotrophusfrom Methanolviathe Entner-Doudoroff Pathway, Originating inEscherichia coli." Bioscience, Biotechnology, and Biochemistry 72, no. 10 (October 23, 2008): 2535–42. http://dx.doi.org/10.1271/bbb.80183.

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26

Goldbourt, Amir, Loren A. Day, and Ann E. McDermott. "Assignment of congested NMR spectra: Carbonyl backbone enrichment via the Entner–Doudoroff pathway." Journal of Magnetic Resonance 189, no. 2 (December 2007): 157–65. http://dx.doi.org/10.1016/j.jmr.2007.07.011.

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27

Olavarria, Karel, Marina Pupke Marone, Henrique da Costa Oliveira, Juan Camilo Roncallo, Fernanda Nogales da Costa Vasconcelos, Luiziana Ferreira da Silva, and José Gregório Cabrera Gomez. "Quantifying NAD(P)H production in the upper Entner-Doudoroff pathway fromPseudomonas putidaKT2440." FEBS Open Bio 5, no. 1 (January 1, 2015): 908–15. http://dx.doi.org/10.1016/j.fob.2015.11.002.

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28

Dhatt, Sharmistha, Shrabani Sen, and Pinaki Chaudhury. "Entner-Doudoroff glycolysis pathway as quadratic-cubic mixed autocatalytic network: A kinetic assay." Chemical Physics 528 (January 2020): 110531. http://dx.doi.org/10.1016/j.chemphys.2019.110531.

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Mardanov, Andrey V., Vitali A. Svetlitchnyi, Alexey V. Beletsky, Maria I. Prokofeva, Elizaveta A. Bonch-Osmolovskaya, Nikolai V. Ravin, and Konstantin G. Skryabin. "The Genome Sequence of the Crenarchaeon Acidilobus saccharovorans Supports a New Order, Acidilobales, and Suggests an Important Ecological Role in Terrestrial Acidic Hot Springs." Applied and Environmental Microbiology 76, no. 16 (June 25, 2010): 5652–57. http://dx.doi.org/10.1128/aem.00599-10.

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ABSTRACT Acidilobus saccharovorans is an anaerobic, organotrophic, thermoacidophilic crenarchaeon isolated from a terrestrial hot spring. We report the complete genome sequence of A. saccharovorans, which has permitted the prediction of genes for Embden-Meyerhof and Entner-Doudoroff pathways and genes associated with the oxidative tricarboxylic acid cycle. The electron transfer chain is branched with two sites of proton translocation and is linked to the reduction of elemental sulfur and thiosulfate. The genomic data suggest an important role of the order Acidilobales in thermoacidophilic ecosystems whereby its members can perform a complete oxidation of organic substrates, closing the anaerobic carbon cycle.

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Roy, Alexander B., Michael J. E. Hewlins, Andrew J. Ellis, John L. Harwood, and Graham F. White. "Glycolytic Breakdown of Sulfoquinovose in Bacteria: a Missing Link in the Sulfur Cycle." Applied and Environmental Microbiology 69, no. 11 (November 2003): 6434–41. http://dx.doi.org/10.1128/aem.69.11.6434-6441.2003.

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ABSTRACT Sulfoquinovose (6-deoxy-6-sulfo-d-glucopyranose), formed by the hydrolysis of the plant sulfolipid, is a major component of the biological sulfur cycle. However, pathways for its catabolism are poorly delineated. We examined the hypothesis that mineralization of sulfoquinovose to inorganic sulfate is initiated by reactions of the glycolytic and/or Entner-Doudoroff pathways in bacteria. Metabolites of [U-13C]sulfoquinovose were identified by 13C-nuclear magnetic resonance (NMR) in strains of Klebsiella and Agrobacterium previously isolated for their ability to utilize sulfoquinovose as a sole source of carbon and energy for growth, and cell extracts were analyzed for enzymes diagnostic for the respective pathways. Klebsiella sp. strain ABR11 grew rapidly on sulfoquinovose, with major accumulations of sulfopropandiol (2,3-dihydroxypropanesulfonate) but no detectable release of sulfate. Later, when sulfoquinovose was exhausted and growth was very slow, sulfopropandiol disappeared and inorganic sulfate and small amounts of sulfolactate (2-hydroxy-3-sulfopropionate) were formed. In Agrobacterium sp. strain ABR2, growth and sulfoquinovose disappearance were again coincident, though slower than that in Klebsiella sp. Release of sulfate was still late but was faster than that in Klebsiella sp., and no metabolites were detected by 13C-NMR. Extracts of both strains grown on sulfoquinovose contained phosphofructokinase activities that remained unchanged when fructose 6-phosphate was replaced in the assay mixture with either glucose 6-phosphate or sulfoquinovose. The results were consistent with the operation of the Embden-Meyerhoff-Parnas (glycolysis) pathway for catabolism of sulfoquinovose. Extracts of Klebsiella but not Agrobacterium also contained an NAD+-dependent sulfoquinovose dehydrogenase activity, indicating that the Entner-Doudoroff pathway might also contribute to catabolism of sulfoquinovose.

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Kouril, Theresa, Patricia Wieloch, Julia Reimann, Michaela Wagner, Melanie Zaparty, Sonja‐Verena Albers, Dietmar Schomburg, Peter Ruoff, and Bettina Siebers. "Unraveling the function of the two Entner–Doudoroff branches in the thermoacidophilic CrenarchaeonSulfolobus solfataricusP2." FEBS Journal 280, no. 4 (January 31, 2013): 1126–38. http://dx.doi.org/10.1111/febs.12106.

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Ng, Chiam Yu, Iman Farasat, Costas D. Maranas, and Howard M. Salis. "Rational design of a synthetic Entner–Doudoroff pathway for improved and controllable NADPH regeneration." Metabolic Engineering 29 (May 2015): 86–96. http://dx.doi.org/10.1016/j.ymben.2015.03.001.

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Rutkis, Reinis, Uldis Kalnenieks, Egils Stalidzans, and David A. Fell. "Kinetic modelling of the Zymomonas mobilis Entner–Doudoroff pathway: insights into control and functionality." Microbiology 159, Pt_12 (December 1, 2013): 2674–89. http://dx.doi.org/10.1099/mic.0.071340-0.

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Liu, Huaiwei, Yuanzhang Sun, Kristine Rose M. Ramos, Grace M. Nisola, Kris Niño G. Valdehuesa, Won–Keun Lee, Si Jae Park, and Wook-Jin Chung. "Combination of Entner-Doudoroff Pathway with MEP Increases Isoprene Production in Engineered Escherichia coli." PLoS ONE 8, no. 12 (December 20, 2013): e83290. http://dx.doi.org/10.1371/journal.pone.0083290.

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Chavarría, Max, Pablo I. Nikel, Danilo Pérez-Pantoja, and Víctor de Lorenzo. "The Entner-Doudoroff pathway empowersPseudomonas putida KT2440 with a high tolerance to oxidative stress." Environmental Microbiology 15, no. 6 (January 10, 2013): 1772–85. http://dx.doi.org/10.1111/1462-2920.12069.

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Rutkis, Reinis, Inese Strazdina, Elina Balodite, Zane Lasa, Nina Galinina, and Uldis Kalnenieks. "The Low Energy-Coupling Respiration in Zymomonas mobilis Accelerates Flux in the Entner-Doudoroff Pathway." PLOS ONE 11, no. 4 (April 21, 2016): e0153866. http://dx.doi.org/10.1371/journal.pone.0153866.

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Borodina, Irina, Charlotte Schöller, Anna Eliasson, and Jens Nielsen. "Metabolic Network Analysis of Streptomyces tenebrarius, a Streptomyces Species with an Active Entner-Doudoroff Pathway." Applied and Environmental Microbiology 71, no. 5 (May 2005): 2294–302. http://dx.doi.org/10.1128/aem.71.5.2294-2302.2005.

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ABSTRACT Streptomyces tenebrarius is an industrially important microorganism, producing an antibiotic complex that mainly consists of the aminoglycosides apramycin, tobramycin carbamate, and kanamycin B carbamate. When S. tenebrarius is used for industrial tobramycin production, kanamycin B carbamate is an unwanted by-product. The two compounds differ only by one hydroxyl group, which is present in kanamycin carbamate but is reduced during biosynthesis of tobramycin. 13C metabolic flux analysis was used for elucidating connections between the primary carbon metabolism and the composition of the antibiotic complex. Metabolic flux maps were constructed for the cells grown on minimal medium with glucose or with a glucose-glycerol mixture as the carbon source. The addition of glycerol, which is more reduced than glucose, led to a three-times-greater reduction of the kanamycin portion of the antibiotic complex. The labeling indicated an active Entner-Doudoroff (ED) pathway, which was previously considered to be nonfunctional in Streptomyces. The activity of the pentose phosphate (PP) pathway was low (10 to 20% of the glucose uptake rate). The fluxes through Embden-Meyerhof-Parnas (EMP) and ED pathways were almost evenly distributed during the exponential growth on glucose. During the transition from growth phase to production phase, a metabolic shift was observed, characterized by a decreased flux through the ED pathway and increased fluxes through the EMP and PP pathways. Higher specific NADH and NADPH production rates were calculated in the cultivation on glucose-glycerol, which was associated with a lower percentage of nonreduced antibiotic kanamycin B carbamate.

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KIM, Seonghun, and Sun Bok LEE. "Characterization ofSulfolobus solfataricus2-Keto-3-deoxy-D-gluconate Kinase in the Modified Entner-Doudoroff Pathway." Bioscience, Biotechnology, and Biochemistry 70, no. 6 (June 23, 2006): 1308–16. http://dx.doi.org/10.1271/bbb.50566.

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Budgen, Nigel, and Michael J. Danson. "Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium Thermoplasma acidophilum." FEBS Letters 196, no. 2 (February 17, 1986): 207–10. http://dx.doi.org/10.1016/0014-5793(86)80247-2.

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DANDEKAR, Thomas, Stefan SCHUSTER, Berend SNEL, Martijn HUYNEN, and Peer BORK. "Pathway alignment: application to the comparative analysis of glycolytic enzymes." Biochemical Journal 343, no. 1 (September 24, 1999): 115–24. http://dx.doi.org/10.1042/bj3430115.

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Comparative analysis of metabolic pathways in different genomes yields important information on their evolution, on pharmacological targets and on biotechnological applications. In this study on glycolysis, three alternative ways of comparing biochemical pathways are combined: (1) analysis and comparison of biochemical data, (2) pathway analysis based on the concept of elementary modes, and (3) a comparative genome analysis of 17 completely sequenced genomes. The analysis reveals a surprising plasticity of the glycolytic pathway. Isoenzymes in different species are identified and compared; deviations from the textbook standard are detailed. Several potential pharmacological targets and by-passes (such as the Entner-Doudoroff pathway) to glycolysis are examined and compared in the different species. Archaean, bacterial and parasite specific adaptations are identified and described.

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KIM, Seonghun, and Sun Bok LEE. "Identification and characterization of Sulfolobus solfataricusD-gluconate dehydratase: a key enzyme in the non-phosphorylated Entner–Doudoroff pathway." Biochemical Journal 387, no. 1 (March 22, 2005): 271–80. http://dx.doi.org/10.1042/bj20041053.

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The extremely thermoacidophilic archaeon Sulfolobus solfataricus utilizes D-glucose as a sole carbon and energy source through the non-phosphorylated Entner–Doudoroff pathway. It has been suggested that this micro-organism metabolizes D-gluconate, the oxidized form of D-glucose, to pyruvate and D-glyceraldehyde by using two unique enzymes, D-gluconate dehydratase and 2-keto-3-deoxy-D-gluconate aldolase. In the present study, we report the purification and characterization of D-gluconate dehydratase from S. solfataricus, which catalyses the conversion of D-gluconate into 2-keto-3-deoxy-D-gluconate. D-Gluconate dehydratase was purified 400-fold from extracts of S. solfataricus by ammonium sulphate fractionation and chromatography on DEAE-Sepharose, Q-Sepharose, phenyl-Sepharose and Mono Q. The native protein showed a molecular mass of 350 kDa by gel filtration, whereas SDS/PAGE analysis provided a molecular mass of 44 kDa, indicating that D-gluconate dehydratase is an octameric protein. The enzyme showed maximal activity at temperatures between 80 and 90 °C and pH values between 6.5 and 7.5, and a half-life of 40 min at 100 °C. Bivalent metal ions such as Co2+, Mg2+, Mn2+ and Ni2+ activated, whereas EDTA inhibited the enzyme. A metal analysis of the purified protein revealed the presence of one Co2+ ion per enzyme monomer. Of the 22 aldonic acids tested, only D-gluconate served as a substrate, with Km=0.45 mM and Vmax=0.15 unit/mg of enzyme. From N-terminal sequences of the purified enzyme, it was found that the gene product of SSO3198 in the S. solfataricus genome database corresponded to D-gluconate dehydratase (gnaD). We also found that the D-gluconate dehydratase of S. solfataricus is a phosphoprotein and that its catalytic activity is regulated by a phosphorylation–dephosphorylation mechanism. This is the first report on biochemical and genetic characterization of D-gluconate dehydratase involved in the non-phosphorylated Entner–Doudoroff pathway.

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VERHEES, Corné H., Servé W. M. KENGEN, Judith E. TUININGA, Gerrit J. SCHUT, Michael W. W. ADAMS, Willem M. de VOS, and John van der OOST. "The unique features of glycolytic pathways in Archaea." Biochemical Journal 375, no. 2 (October 15, 2003): 231–46. http://dx.doi.org/10.1042/bj20021472.

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An early divergence in evolution has resulted in two prokaryotic domains, the Bacteria and the Archaea. Whereas the central metabolic routes of bacteria and eukaryotes are generally well-conserved, variant pathways have developed in Archaea involving several novel enzymes with a distinct control. A spectacular example of convergent evolution concerns the glucose-degrading pathways of saccharolytic archaea. The identification, characterization and comparison of the glycolytic enzymes of a variety of phylogenetic lineages have revealed a mosaic of canonical and novel enzymes in the archaeal variants of the Embden–Meyerhof and the Entner–Doudoroff pathways. By means of integrating results from biochemical and genetic studies with recently obtained comparative and functional genomics data, the structure and function of the archaeal glycolytic routes, the participating enzymes and their regulation are re-evaluated.

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Sonawat, Haripalsingh M., Sudha Srivastava, S. Swaminathan, and Girjesh Govil. "Glycolysis and Entner-Doudoroff pathways in Halobacterium halobium: Some new observations based on 13C NMR spectroscopy." Biochemical and Biophysical Research Communications 173, no. 1 (November 1990): 358–62. http://dx.doi.org/10.1016/s0006-291x(05)81065-4.

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Refaeli, Bosmat, and Amir Goldbourt. "Protein expression and isotopic enrichment based on induction of the Entner–Doudoroff pathway in Escherichia coli." Biochemical and Biophysical Research Communications 427, no. 1 (October 2012): 154–58. http://dx.doi.org/10.1016/j.bbrc.2012.09.031.

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Carter, A. T., B. M. Pearson, J. R. Dickinson, and W. E. Lancashire. "Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-Doudoroff pathway." Gene 130, no. 1 (August 1993): 155–56. http://dx.doi.org/10.1016/0378-1119(93)90362-7.

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46

George, Andrée S., Isai Salas González, Graciela L. Lorca, and Max Teplitski. "Contribution of the Salmonella enterica KdgR Regulon to Persistence of the Pathogen in Vegetable Soft Rots." Applied and Environmental Microbiology 82, no. 4 (December 18, 2015): 1353–60. http://dx.doi.org/10.1128/aem.03355-15.

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ABSTRACTDuring their colonization of plants, human enteric pathogens, such asSalmonella enterica, are known to benefit from interactions with phytopathogens. At least in part, benefits derived bySalmonellafrom the association with a soft rot caused byPectobacterium carotovorumwere shown to be dependent onSalmonellaKdgR, a regulator of genes involved in the uptake and utilization of carbon sources derived from the degradation of plant polymers. ASalmonellakdgRmutant was more fit in soft rots but not in the lesions caused byXanthomonasspp. andPseudomonasspp. Bioinformatic, phenotypic, and gene expression analyses demonstrated that the KdgR regulon included genes involved in uptake and metabolism of molecules resulting from pectin degradation as well as those central to the utilization of a number of other carbon sources. Mutant analyses indicated that the Entner-Doudoroff pathway, in part controlled by KdgR, was critical for the persistence within soft rots and likely was responsible for thekdgRphenotype.

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Theodossis, Alex, Christine C. Milburn, Narinder I. Heyer, Henry J. Lamble, David W. Hough, Michael J. Danson, and Garry L. Taylor. "Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner–Doudoroff pathway in the hyperthermophilic archaeonSulfolobus solfataricus." Acta Crystallographica Section F Structural Biology and Crystallization Communications 61, no. 1 (December 24, 2004): 112–15. http://dx.doi.org/10.1107/s174430910403101x.

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48

Harada, Eiji, Ken-Ichiro Iida, Susumu Shiota, Hiroaki Nakayama, and Shin-Ichi Yoshida. "Glucose Metabolism in Legionella pneumophila: Dependence on the Entner-Doudoroff Pathway and Connection with Intracellular Bacterial Growth." Journal of Bacteriology 192, no. 11 (April 2, 2010): 2892–99. http://dx.doi.org/10.1128/jb.01535-09.

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ABSTRACT Glucose metabolism in Legionella pneumophila was studied by focusing on the Entner-Doudoroff (ED) pathway with a combined genetic and biochemical approach. The bacterium utilized exogenous glucose for synthesis of acid-insoluble cell components but manifested no discernible increase in the growth rate. Assays with permeabilized cell preparations revealed the activities of three enzymes involved in the pathway, i.e., glucokinase, phosphogluconate dehydratase, and 2-dehydro-3-deoxy-phosphogluconate aldolase, presumed to be encoded by the glk, edd, and eda genes, respectively. Gene-disrupted mutants for the three genes and the ywtG gene encoding a putative sugar transporter were devoid of the ability to metabolize exogenous glucose, indicating that the pathway is almost exclusively responsible for glucose metabolism and that the ywtG gene product is the glucose transporter. It was also established that these four genes formed part of an operon in which the gene order was edd-glk-eda-ywtG, as predicted by genomic information. Intriguingly, while the mutants exhibited no appreciable change in growth characteristics in vitro, they were defective in multiplication within eukaryotic cells, strongly indicating that the ED pathway must be functional for the intracellular growth of the bacterium to occur. Curiously, while the deficient glucose metabolism of the ywtG mutant was successfully complemented by the ywtG + gene supplied in trans via plasmid, its defect in intracellular growth was not. However, the latter defect was also manifested in wild-type cells when a plasmid carrying the mutant ywtG gene was introduced. This phenomenon, resembling so-called dominant negativity, awaits further investigation.

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Patra, T., H. Koley, T. Ramamurthy, A. C. Ghose, and R. K. Nandy. "The Entner-Doudoroff Pathway Is Obligatory for Gluconate Utilization and Contributes to the Pathogenicity of Vibrio cholerae." Journal of Bacteriology 194, no. 13 (April 27, 2012): 3377–85. http://dx.doi.org/10.1128/jb.06379-11.

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Selig, Martina, Karina B. Xavier, Helena Santos, and Peter Schönheit. "Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga." Archives of Microbiology 167, no. 4 (November 4, 1996): 217–32. http://dx.doi.org/10.1007/bf03356097.

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