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Journal articles on the topic 'Phosphoenolpyruvate -phosphotransferase system'

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Published: 6 September 2023

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1

Navdaeva, Vera, Andreas Zurbriggen, Sandro Waltersperger, Philipp Schneider, Anselm E. Oberholzer, Priska Bähler, Christoph Bächler, Andreas Grieder, Ulrich Baumann, and Bernhard Erni. "Phosphoenolpyruvate: Sugar Phosphotransferase System from the HyperthermophilicThermoanaerobacter tengcongensis." Biochemistry 50, no. 7 (February 22, 2011): 1184–93. http://dx.doi.org/10.1021/bi101721f.

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2

Anderson, J. W. "HPr: a model protein." Biochemistry and Cell Biology 73, no. 5-6 (May 1, 1995): 219–22. http://dx.doi.org/10.1139/o95-026.

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Histidine-containing protein (HPr) is a central component of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS). This brief review covers recent structure–function studies on the active center of this protein: the role of the active center residues in phosphotransfer; the residues contributing to the phosphohydrolysis properties of HPr; and the contribution residues in HPr make to the pKaof the transiently phosphorylated active-site residue, His 15. As well, the potential for HPr to be used as a model protein for studying problems not directly associated with its function in the PTS is discussed.Key words: phosphoenolpyruvate: sugar phosphotransferase system, histidine-containing protein, active center, structure–function, model protein.

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3

Horng, Yu-Tze, Chi-Jen Wang, Wen-Ting Chung, Huei-Jen Chao, Yih-Yuan Chen, and Po-Chi Soo. "Phosphoenolpyruvate phosphotransferase system components positively regulate Klebsiella biofilm formation." Journal of Microbiology, Immunology and Infection 51, no. 2 (April 2018): 174–83. http://dx.doi.org/10.1016/j.jmii.2017.01.007.

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4

Tarshis, Mark. "Spiroplasma cells utilize carbohydrates via the phosphoenolpyruvate-dependent sugar phosphotransferase system." Canadian Journal of Microbiology 37, no. 6 (June 1, 1991): 477–79. http://dx.doi.org/10.1139/m91-079.

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Ten Spiroplasma species tested were found capable of fermenting glucose, mannose, fructose, and sucrose, but not ribose, maltose, 2-deoxyglucose, xylose, sorbitol, glactose, lactose, and arabinose. Sugar utilization was measured by a direct measurement of the changes in pH of a washed cell suspension upon the addition of the various sugars. Sulfhydryl reagents, uncouplers, and glycolysis inhibitors prevented the sugar-induced pH shifts. The spiroplasmas were capable of phosporylating α-methylgucoside in a reaction that required phosphoenolypyruvate, but not ATP, as a phosphate donor, suggesting that Spiroplasma species possess a phosphoenolpyruvate-dependent sugar phosphotransferase system. Key words: Spiroplasma, carbohydrate utilization, pH changes, phosphenolpyruvate-dependent sugar phosphotransferase system.

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5

Vadeboncoeur, Christian, and Lucie Gauthier. "The phosphoenolpyruvate: sugar phosphotransferase system of Streptococcus salivarius. Identification of a IIIman protein." Canadian Journal of Microbiology 33, no. 2 (February 1, 1987): 118–22. http://dx.doi.org/10.1139/m87-020.

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A double-spontaneous mutant resistant to the growth inhibitory effect of α-methylglucoside and 2-deoxyglucose was isolated from Streptococcus salivarius. This mutant strain, called αS3L11, did not grow on mannose and grew poorly on 5 mM fructose and 5 mM glucose. Isolated membranes of strain αS3L11 were unable to catalyse the phosphoenolpyruvate-dependent phosphorylation of mannose in the presence of purified enzyme I and HPr. Addition of dialysed membrane-free cellular extract of the wild-type strain to the reaction medium restored the activity. The factor that restored the phosphoenolpyruvate–mannose phosphotransferase activity to membranes of strain αS3L11 was called IIIman. This factor was partially purified from the wild-type strain by DEAE-cellulose chromatography, DEAE-TSK chromatography, and molecular seiving on a column of Ultrogel AcA 34. This partially purified preparation also enhanced the phosphoenolpyruvate-dependent phosphorylation of glucose, fructose, and 2-deoxyglucose in strain αS3L11.

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6

Aboulwafa, Mohammad, and Milton H. Saier. "Characterization of Soluble Enzyme II Complexes of the Escherichia coli Phosphotransferase System." Journal of Bacteriology 186, no. 24 (December 15, 2004): 8453–62. http://dx.doi.org/10.1128/jb.186.24.8453-8462.2004.

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ABSTRACT Plasmid-encoded His-tagged glucose permease of Escherichia coli, the enzyme IIBCGlc (IIGlc), exists in two physical forms, a membrane-integrated oligomeric form and a soluble monomeric form, which separate from each other on a gel filtration column (peaks 1 and 2, respectively). Western blot analyses using anti-His tag monoclonal antibodies revealed that although IIGlc from the two fractions migrated similarly in sodium dodecyl sulfate gels, the two fractions migrated differently on native gels both before and after Triton X-100 treatment. Peak 1 IIGlc migrated much more slowly than peak 2 IIGlc. Both preparations exhibited both phosphoenolpyruvate-dependent sugar phosphorylation activity and sugar phosphate-dependent sugar transphosphorylation activity. The kinetics of the transphosphorylation reaction catalyzed by the two IIGlc fractions were different: peak 1 activity was subject to substrate inhibition, while peak 2 activity was not. Moreover, the pH optima for the phosphoenolpyruvate-dependent activities differed for the two fractions. The results provide direct evidence that the two forms of IIGlc differ with respect to their physical states and their catalytic activities. These general conclusions appear to be applicable to the His-tagged mannose permease of E. coli. Thus, both phosphoenolpyruvate-dependent phosphotransferase system enzymes exist in soluble and membrane-integrated forms that exhibit dissimilar physical and kinetic properties.

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7

Webb, Alexander J., Karen A. Homer, and Arthur H. F. Hosie. "A Phosphoenolpyruvate-Dependent Phosphotransferase System Is the Principal Maltose Transporter in Streptococcus mutans." Journal of Bacteriology 189, no. 8 (February 2, 2007): 3322–27. http://dx.doi.org/10.1128/jb.01633-06.

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ABSTRACT We report that a phosphoenolpyruvate-dependent phosphotransferase system, MalT, is the principal maltose transporter for Streptococcus mutans. MalT also contributes to maltotriose uptake. Since maltose and maltodextrins are products of starch degradation found in saliva, the ability to take up and ferment these carbohydrates may contribute to dental caries.

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8

Alice, Alejandro F., Gaspar Pérez-Martínez, and Carmen Sánchez-Rivas. "Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine metabolism in Bacillus sphaericus." Microbiology 149, no. 7 (July 1, 2003): 1687–98. http://dx.doi.org/10.1099/mic.0.26231-0.

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Bacillus sphaericus, a bacterium of biotechnological interest due to its ability to produce mosquitocidal toxins, is unable to use sugars as carbon source. However, ptsHI genes encoding HPr and EI proteins belonging to a PTS were cloned, sequenced and characterized. Both HPr and EI proteins were fully functional for phosphoenolpyruvate-dependent transphosphorylation in complementation assays using extracts from Staphylococcus aureus mutants for one of these proteins. HPr(His6) was purified from wild-type and a Ser46/Gln mutant of B. sphaericus, and used for in vitro phosphorylation experiments using extracts from either B. sphaericus or Bacillus subtilis as kinase source. The results showed that both phosphorylated forms, P-Ser46-HPr and P-His15-HPr, could be obtained. The findings also proved indirectly the existence of an HPr kinase activity in B. sphaericus. The genetic structure of these ptsHI genes has some unusual features, as they are co-transcribed with genes encoding metabolic enzymes related to N-acetylglucosamine (GlcNAc) catabolism (nagA, nagB and an undetermined orf2). In fact, this bacterium was able to utilize this amino sugar as carbon and energy source, but a ptsH null mutant had lost this characteristic. Investigation of GlcNAc uptake and streptozotocin inhibition in both a wild-type and a ptsH null mutant strain led to the proposal that GlcNAc is transported and phosphorylated by an EIINag element of the PTS, as yet uncharacterized. In addition, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase activities were determined; both were induced in the presence of GlcNAc. These results, together with the authors' recent findings of the presence of a phosphofructokinase activity, are strongly indicative of a glycolytic pathway in B. sphaericus. They also open new possibilities for genetic improvements in industrial applications.

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9

Siebold, Christian, Karin Flükiger, Rudolf Beutler, and Bernhard Erni. "Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS)." FEBS Letters 504, no. 3 (August 28, 2001): 104–11. http://dx.doi.org/10.1016/s0014-5793(01)02705-3.

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10

Bouvet, O. M. M., and P. A. D. Grimont. "Diversity of the phosphoenolpyruvate/glucose phosphotransferase system in the Enterobacteriaceae." Annales de l'Institut Pasteur / Microbiologie 138, no. 1 (January 1987): 3–13. http://dx.doi.org/10.1016/0769-2609(87)90048-2.

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11

Schönert, Stefan, Sabine Seitz, Holger Krafft, Eva-Anne Feuerbaum, Iris Andernach, Gabriele Witz, and Michael K. Dahl. "Maltose and Maltodextrin Utilization by Bacillus subtilis." Journal of Bacteriology 188, no. 11 (June 1, 2006): 3911–22. http://dx.doi.org/10.1128/jb.00213-06.

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ABSTRACT Bacillus subtilis can utilize maltose and maltodextrins that are derived from polysaccharides, like starch or glycogen. In this work, we show that maltose is taken up by a member of the phosphoenolpyruvate-dependent phosphotransferase system and maltodextrins are taken up by a maltodextrin-specific ABC transporter. Uptake of maltose by the phosphoenolpyruvate-dependent phosphotransferase system is mediated by maltose-specific enzyme IICB (MalP; synonym, GlvC), with an apparent Km of 5 μM and a V max of 91 nmol · min−1 · (1010 CFU)−1. The maltodextrin-specific ABC transporter is composed of the maltodextrin binding protein MdxE (formerly YvdG), with affinities in the low micromolar range for maltodextrins, and the membrane-spanning components MdxF and MdxG (formerly YvdH and YvdI, respectively), as well as the energizing ATPase MsmX. Maltotriose transport occurs with an apparent Km of 1.4 μM and a V max of 4.7 nmol · min−1 · (1010 CFU)−1.

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12

Velázquez, Francisco, Katharina Pflüger, Ildefonso Cases, Laura I. De Eugenio, and Víctor de Lorenzo. "The Phosphotransferase System Formed by PtsP, PtsO, and PtsN Proteins Controls Production of Polyhydroxyalkanoates in Pseudomonas putida." Journal of Bacteriology 189, no. 12 (April 6, 2007): 4529–33. http://dx.doi.org/10.1128/jb.00033-07.

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ABSTRACT The genome of Pseudomonas putida KT2440 encodes five proteins of the phosphoenolpyruvate-carbohydrate phosphotransferase system. Two of these (FruA and FruB) form a dedicated system for fructose intake, while enzyme INtr (EINtr; encoded by ptsP), NPr (ptsO), and EIINtr (ptsN) act in concert to control the intracellular accumulation of polyhydroxyalkanoates, a typical product of carbon overflow.

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13

Saier, M. H., M. Yamada, B. Erni, K. Suda, J. Lengeler, R. Ebner, R. Argos, et al. "Sugar permeases of the bacterial phosphoenolpyruvate‐dependent phosphotransferase system: sequence comparisons." FASEB Journal 2, no. 3 (March 1988): 199–208. http://dx.doi.org/10.1096/fasebj.2.3.2832233.

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14

Peterkofsky, Alan, Ingrid Svenson, and Niranjana Amin. "Regulation ofEscherichia coliadenylate cyclase activity by the phosphoenolpyruvate: sugar phosphotransferase system." FEMS Microbiology Letters 63, no. 1-2 (June 1989): 103–8. http://dx.doi.org/10.1111/j.1574-6968.1989.tb14105.x.

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15

Ginsburg, Ann, and Alan Peterkofsky. "Enzyme I: The Gateway to the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System." Archives of Biochemistry and Biophysics 397, no. 2 (January 2002): 273–78. http://dx.doi.org/10.1006/abbi.2001.2603.

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16

Zhang, X., K. Jantama, K. T. Shanmugam, and L. O. Ingram. "Reengineering Escherichia coli for Succinate Production in Mineral Salts Medium." Applied and Environmental Microbiology 75, no. 24 (October 16, 2009): 7807–13. http://dx.doi.org/10.1128/aem.01758-09.

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ABSTRACT The fermentative metabolism of glucose was redirected to succinate as the primary product without mutating any genes encoding the native mixed-acid fermentation pathway or redox reactions. Two changes in peripheral pathways were together found to increase succinate yield fivefold: (i) increased expression of phosphoenolpyruvate carboxykinase and (ii) inactivation of the glucose phosphoenolpyruvate-dependent phosphotransferase system. These two changes increased net ATP production, increased the pool of phosphoenolpyruvate available for carboxylation, and increased succinate production. Modest further improvements in succinate yield were made by inactivating the pflB gene, encoding pyruvate formate lyase, resulting in an E scherichia coli pathway that is functionally similar to the native pathway in Actinobacillus succinogenes and other succinate-producing rumen bacteria.

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17

Pérez-Morales, Deyanira, and Víctor H. Bustamante. "The global regulatory system Csr senses glucose through the phosphoenolpyruvate: carbohydrate phosphotransferase system." Molecular Microbiology 99, no. 4 (December 22, 2015): 623–26. http://dx.doi.org/10.1111/mmi.13285.

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18

Kim, Jong Rea, Se Hyeuk Kim, and Pyung Cheon Lee. "Comparison of a phosphoenolpyruvate-dependent phosphotransferase system and a non-phosphotransferase system for sucrose in metabolically engineered Escherichia coli." Journal of Bioscience and Bioengineering 108 (November 2009): S171—S172. http://dx.doi.org/10.1016/j.jbiosc.2009.08.466.

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19

Khajanchi, Bijay K., Evelyn Odeh, Lihui Gao, Mary B. Jacobs, Mario T. Philipp, Tao Lin, and Steven J. Norris. "Phosphoenolpyruvate Phosphotransferase System Components Modulate Gene Transcription and Virulence of Borrelia burgdorferi." Infection and Immunity 84, no. 3 (December 28, 2015): 754–64. http://dx.doi.org/10.1128/iai.00917-15.

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The phosphoenolpyruvate phosphotransferase system (PEP-PTS) and adenylate cyclase (AC) IV (encoded by BB0723 [cyaB]) are well conserved in different species ofBorrelia. However, the functional roles of PEP-PTS and AC in the infectious cycle ofBorreliahave not been characterized previously. We examined 12 PEP-PTS transporter component mutants by needle inoculation of mice to assess their ability to cause mouse infection. Transposon mutants with mutations in the EIIBC components (ptsG) (BB0645, thought to be involved in glucose-specific transport) were unable to cause infection in mice, while all other tested PEP-PTS mutants retained infectivity. Infectivity was partially restored in an intrans-complemented strain of theptsGmutant. While theptsGmutant survived normally in unfed as well as fed ticks, it was unable to cause infection in mice by tick transmission, suggesting that the function ofptsGis essential to establish infection by either needle inoculation or tick transmission. In Gram-negative organisms, the regulatory effects of the PEP-PTS are mediated by adenylate cyclase and cyclic AMP (cAMP) levels. A recombinant protein encoded byB. burgdorferiBB0723 (a putativecyaBhomolog) was shown to have adenylate cyclase activityin vitro; however, mutants with mutations in this gene were fully infectious in the tick-mouse infection cycle, indicating that its function is not required in this process. By transcriptome analysis, we demonstrated that theptsGgene may directly or indirectly modulate gene expression ofBorrelia burgdorferi. Overall, the PEP-PTS glucose transporter PtsG appears to play important roles in the pathogenesis ofB. burgdorferithat extend beyond its transport functions.

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20

Galinier, Anne, and Josef Deutscher. "Sophisticated Regulation of Transcriptional Factors by the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System." Journal of Molecular Biology 429, no. 6 (March 2017): 773–89. http://dx.doi.org/10.1016/j.jmb.2017.02.006.

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21

Johnson, Mark S., Edward H. Rowsell, and Barry L. Taylor. "Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system." FEBS Letters 374, no. 2 (October 30, 1995): 161–64. http://dx.doi.org/10.1016/0014-5793(95)01097-x.

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22

Márquez, JoséA, Stefan Reinelt, Brigitte Koch, Roswitha Engelmann, Wolfgang Hengstenberg, and Klaus Scheffzek. "Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System." Journal of Biological Chemistry 281, no. 43 (July 25, 2006): 32508–15. http://dx.doi.org/10.1074/jbc.m513721200.

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Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphorylates the heat-stable phospho carrier protein at His-15 using PEP as a phosphoryl donor in a reaction that requires EI dimerization and autophosphorylation at His-190. The structure of the full-length protein from Staphylococcus carnosus at 2.5Å reveals an extensive interaction surface between two molecules in adjacent asymmetric units. Structural comparison with related domains indicates that this surface represents the biochemically relevant contact area of dimeric EI. Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region. The large distance of more than 35Å between the active site His-190 and the PEP binding site suggests that large conformational changes must occur during the process of autophosphorylation, as has been proposed for the structurally related enzyme pyruvate phosphate dikinase. Our structure for the first time offers a framework to analyze a large amount of research in the context of the full-length model.

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23

Kajikawa, Hiroshi, and Shigehiko Masaki. "Cellobiose Transport by Mixed Ruminal Bacteria from a Cow." Applied and Environmental Microbiology 65, no. 6 (June 1, 1999): 2565–69. http://dx.doi.org/10.1128/aem.65.6.2565-2569.1999.

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ABSTRACT The transport of cellobiose in mixed ruminal bacteria harvested from a holstein cow fed an Italian ryegrass hay was determined in the presence of nojirimycin-1-sulfate, which almost inhibited cellobiase activity. The kinetic parameters of cellobiose uptake were 14 μM for the Km and 10 nmol/min/mg of protein for theV max. Extracellular and cell-associated cellobiases were detected in the rumen, with both showing higherV max values and lower affinities than those determined for cellobiose transport. The proportion of cellobiose that was directly transported before it was extracellularly degraded into glucose increased as the cellobiose concentration decreased, reaching more than 20% at the actually observed levels of cellobiose in the rumen, which were less than 0.02 mM. The inhibitor experiment showed that cellobiose was incorporated into the cells mainly by the phosphoenolpyruvate phosphotransferase system and partially by an ATP-dependent and proton-motive-force-independent active transport system. This finding was also supported by determinations of phosphoenolpyruvate phosphotransferase-dependent NADH oxidation with cellobiose and the effects of artificial potentials on cellobiose transport. Cellobiose uptake was sensitive to a decrease in pH (especially below 6.0), and it was weakly but significantly inhibited in the presence of glucose.

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24

Pelletier, G., M. Frenette, and C. Vadeboncoeur. "Transport of mannose by an inducible phosphoenolpyruvate: fructose phosphotransferase system in Streptococcus salivarius." Microbiology 140, no. 9 (September 1, 1994): 2433–38. http://dx.doi.org/10.1099/13500872-140-9-2433.

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25

Leng, Yuanyuan, Christopher A. Vakulskas, Tesfalem R. Zere, Bradley S. Pickering, Paula I. Watnick, Paul Babitzke, and Tony Romeo. "Regulation of CsrB/C sRNA decay by EIIAGlcof the phosphoenolpyruvate: carbohydrate phosphotransferase system." Molecular Microbiology 99, no. 4 (November 17, 2015): 627–39. http://dx.doi.org/10.1111/mmi.13259.

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26

Houot, Laetitia, Sarah Chang, Bradley S. Pickering, Cedric Absalon, and Paula I. Watnick. "The Phosphoenolpyruvate Phosphotransferase System Regulates Vibrio cholerae Biofilm Formation through Multiple Independent Pathways." Journal of Bacteriology 192, no. 12 (April 16, 2010): 3055–67. http://dx.doi.org/10.1128/jb.00213-10.

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ABSTRACT The bacterial phosphoenolpyruvate phosphotransferase system (PTS) is a highly conserved phosphotransfer cascade that participates in the transport and phosphorylation of selected carbohydrates and modulates many cellular functions in response to carbohydrate availability. It plays a role in the virulence of many bacterial pathogens. Components of the carbohydrate-specific PTS include the general cytoplasmic components enzyme I (EI) and histidine protein (HPr), the sugar-specific cytoplasmic components enzymes IIA (EIIA) and IIB (EIIB), and the sugar-specific membrane-associated multisubunit components enzymes IIC (EIIC) and IID (EIID). Many bacterial genomes also encode a parallel PTS pathway that includes the EI homolog EINtr, the HPr homolog NPr, and the EIIA homolog EIIANtr. This pathway is thought to be nitrogen specific because of the proximity of the genes encoding this pathway to the genes encoding the nitrogen-specific σ factor σ54. We previously reported that phosphorylation of HPr and FPr by EI represses Vibrio cholerae biofilm formation in minimal medium supplemented with glucose or pyruvate. Here we report two additional PTS-based biofilm regulatory pathways that are active in LB broth but not in minimal medium. These pathways involve the glucose-specific enzyme EIIA (EIIAGlc) and two nitrogen-specific EIIA homologs, EIIANtr1 and EIIANtr2. The presence of multiple, independent biofilm regulatory circuits in the PTS supports the hypothesis that the PTS and PTS-dependent substrates have a central role in sensing environments suitable for a surface-associated existence.

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Kalbitzer, H. R., H. P. Muss, R. Engelmann, H. H. Kiltz, K. Stueber, and W. Hengstenberg. "Phosphoenolpyruvate-dependent phosphotransferase system. Proton NMR studies on chemically modified heat-stable proteins." Biochemistry 24, no. 17 (August 1985): 4562–69. http://dx.doi.org/10.1021/bi00338a012.

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28

Navas-Castillo, J., F. Laigret, A. Hocquellet, C. J. Chang, and J. M. Bove. "Evidence for a phosphoenolpyruvate dependent sugar-phosphotransferase system in the mollicute Acholeplasma florum." Biochimie 75, no. 8 (January 1993): 675–79. http://dx.doi.org/10.1016/0300-9084(93)90098-d.

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29

Hu, Kuang-Yu, and Milton H. Saier. "Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system." Research in Microbiology 153, no. 7 (September 2002): 405–15. http://dx.doi.org/10.1016/s0923-2508(02)01339-6.

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30

Kornberg, H. L., L. T. M. Lambourne, and A. A. Sproul. "Facilitated diffusion of fructose via the phosphoenolpyruvate/glucose phosphotransferase system of Escherichia coli." Proceedings of the National Academy of Sciences 97, no. 4 (February 15, 2000): 1808–12. http://dx.doi.org/10.1073/pnas.97.4.1808.

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31

NELSON, Stephen O., Anja R. J. SCHUITEMA, and Pieter W. POSTMA. "The phosphoenolpyruvate: glucose phosphotransferase system of Salmonella typhimurium. The phosphorylated form of IIIGlc." European Journal of Biochemistry 154, no. 2 (January 1986): 337–41. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09402.x.

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32

Pflüger-Grau, Katharina, and Víctor de Lorenzo. "From the phosphoenolpyruvate phosphotransferase system to selfish metabolism: a story retraced inPseudomonas putida." FEMS Microbiology Letters 356, no. 2 (May 29, 2014): 144–53. http://dx.doi.org/10.1111/1574-6968.12459.

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33

PETERKOFSKY, A. "Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate: Sugar phosphotransferase system." FEMS Microbiology Reviews 63, no. 1-2 (June 1989): 103–8. http://dx.doi.org/10.1016/0168-6445(89)90013-2.

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34

Humphries, Romney M., Theodoros Kelesidis, Ryan Tewhey, Warren E. Rose, Nicholas Schork, Victor Nizet, and George Sakoulas. "Genotypic and Phenotypic Evaluation of the Evolution of High-Level Daptomycin Nonsusceptibility in Vancomycin-Resistant Enterococcus faecium." Antimicrobial Agents and Chemotherapy 56, no. 11 (September 4, 2012): 6051–53. http://dx.doi.org/10.1128/aac.01318-12.

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ABSTRACTWhole-genome sequencing and cell membrane studies of three clonalEnterococcus faeciumstrains with daptomycin MICs of 4, 32, and 192 μg/ml were performed, revealing nonsynonymous single nucleotide variants in eight open reading frames, including those predicted to encode a phosphoenolpyruvate-dependent, mannose-specific phosphotransferase system, cardiolipin synthetase, and EzrA. Membrane studies revealed a higher net surface charge among the daptomycin-nonsusceptible isolates and increased septum formation in the isolate with a daptomycin MIC of 192 μg/ml.

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35

Barabote, Ravi D., and Milton H. Saier. "Comparative Genomic Analyses of the Bacterial Phosphotransferase System." Microbiology and Molecular Biology Reviews 69, no. 4 (December 2005): 608–34. http://dx.doi.org/10.1128/mmbr.69.4.608-634.2005.

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SUMMARY We report analyses of 202 fully sequenced genomes for homologues of known protein constituents of the bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS). These included 174 bacterial, 19 archaeal, and 9 eukaryotic genomes. Homologues of PTS proteins were not identified in archaea or eukaryotes, showing that the horizontal transfer of genes encoding PTS proteins has not occurred between the three domains of life. Of the 174 bacterial genomes (136 bacterial species) analyzed, 30 diverse species have no PTS homologues, and 29 species have cytoplasmic PTS phosphoryl transfer protein homologues but lack recognizable PTS permeases. These soluble homologues presumably function in regulation. The remaining 77 species possess all PTS proteins required for the transport and phosphorylation of at least one sugar via the PTS. Up to 3.2% of the genes in a bacterium encode PTS proteins. These homologues were analyzed for family association, range of protein types, domain organization, and organismal distribution. Different strains of a single bacterial species often possess strikingly different complements of PTS proteins. Types of PTS protein domain fusions were analyzed, showing that certain types of domain fusions are common, while others are rare or prohibited. Select PTS proteins were analyzed from different phylogenetic standpoints, showing that PTS protein phylogeny often differs from organismal phylogeny. The results document the frequent gain and loss of PTS protein-encoding genes and suggest that the lateral transfer of these genes within the bacterial domain has played an important role in bacterial evolution. Our studies provide insight into the development of complex multicomponent enzyme systems and lead to predictions regarding the types of protein-protein interactions that promote efficient PTS-mediated phosphoryl transfer.

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36

Lee, Jieun, Wilfrid J. Mitchell, Martin Tangney, and H. P. Blaschek. "Evidence for the Presence of an Alternative Glucose Transport System in Clostridium beijerinckii NCIMB 8052 and the Solvent-Hyperproducing Mutant BA101." Applied and Environmental Microbiology 71, no. 6 (June 2005): 3384–87. http://dx.doi.org/10.1128/aem.71.6.3384-3387.2005.

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ABSTRACT The effects of substrate analogs and energy inhibitors on glucose uptake and phosphorylation by Clostridium beijerinckii provide evidence for the operation of two uptake systems: a previously characterized phosphoenolpyruvate-dependent phosphotransferase system (PTS) and a non-PTS system probably energized by the transmembrane proton gradient. In both wild-type C. beijerinckii NCIMB 8052 and the butanol-hyperproducing mutant BA101, PTS activity declined at the end of exponential growth, while glucokinase activity increased in the later stages of fermentation. The non-PTS uptake system, together with enhanced glucokinase activity, may provide an explanation for the ability of the mutant to utilize glucose more effectively during fermentation despite the fact that it is partially defective in PTS activity.

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37

Galperin, MY, KM Noll, and AH Romano. "The glucose transport system of the hyperthermophilic anaerobic bacterium Thermotoga neapolitana." Applied and Environmental Microbiology 62, no. 8 (August 1996): 2915–18. http://dx.doi.org/10.1128/aem.62.8.2915-2918.1996.

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The glucose transport system of the extremely thermophilic anaerobic bacterium Thermotoga neapolitana was studied with the nonmetabolizable glucose analog 2-deoxy-D-glucose (2-DOG). T. neapolitana accumulated 2-DOG against a concentration gradient in an intracellular free sugar pool that was exchangeable with external source of energy, such as pyruvate, and was inhibited by arsenate and gramicidin D. There was no phosphoenolpyruvate-dependent phosphorylation of glucose, 2-DOG, or fructose by cell extracts or toluene-treated cells, indicating the absence of a phosphoenolpyruvate:sugar phosphotransferase system. These data indicate that D-glucose is taken up by T. neapolitana via an active transport system that is energized by an ion gradient generated by ATP, derived from substrate-level phosphorylation.

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38

LOLKEMA, Juke S., Ria H. ten HOEVE-DUURKENS, and George T. ROBILLARD. "The phosphoenolpyruvate-dependent fructose-specific phosphotransferase system in Rhodopseudomonas sphaeroide. Energetics of the phosphoryl group transfer from phosphoenolpyruvate to fructose." European Journal of Biochemistry 154, no. 2 (January 1986): 387–93. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09410.x.

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39

Martin, S. A., and J. B. Russell. "Phosphoenolpyruvate-dependent phosphorylation of hexoses by ruminal bacteria: evidence for the phosphotransferase transport system." Applied and Environmental Microbiology 52, no. 6 (1986): 1348–52. http://dx.doi.org/10.1128/aem.52.6.1348-1352.1986.

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40

Thompson, J., and B. M. Chassy. "Intracellular phosphorylation of glucose analogs via the phosphoenolpyruvate: mannose-phosphotransferase system in Streptococcus lactis." Journal of Bacteriology 162, no. 1 (1985): 224–34. http://dx.doi.org/10.1128/jb.162.1.224-234.1985.

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41

Gershanovitch, V. N., T. N. Bolshakova, M. L. Molchanova, A. M. Umyarov, O. Yu Dobrynina, Yu A. Grigorenko, and R. S. Erlagaeva. "Fructose-specific phosphoenolpyruvate dependent phosphotransferase system ofEscherichia coli: its alterations and adenylate cyclase activity." FEMS Microbiology Letters 63, no. 1-2 (June 1989): 125–33. http://dx.doi.org/10.1111/j.1574-6968.1989.tb14108.x.

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42

Pereira, Catarina S., António J. M. Santos, Michal Bejerano-Sagie, Paulo B. Correia, Joao C. Marques, and Karina B. Xavier. "Phosphoenolpyruvate phosphotransferase system regulates detection and processing of the quorum sensing signal autoinducer-2." Molecular Microbiology 84, no. 1 (March 5, 2012): 93–104. http://dx.doi.org/10.1111/j.1365-2958.2012.08010.x.

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43

Pereira, Catarina S., António J. M. Santos, Michal Bejerano-Sagie, Paulo B. Correia, Joao C. Marques, and Karina B. Xavier. "Phosphoenolpyruvate phosphotransferase system regulates detection and processing of the quorum sensing signal autoinducer-2." Molecular Microbiology 85, no. 4 (August 2012): 815. http://dx.doi.org/10.1111/j.1365-2958.2012.08161.x.

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44

Waygood, E. Bruce, Ellen Erickson, Ossama A. L. El-Kabbani, and Louis T. J. Delbaere. "Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate/sugar phosphotransferase system." Biochemistry 24, no. 24 (November 1985): 6938–45. http://dx.doi.org/10.1021/bi00345a028.

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45

Tanaka, Yuya, Haruhiko Teramoto, Masayuki Inui, and Hideaki Yukawa. "Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R." Microbiology 155, no. 11 (November 1, 2009): 3652–60. http://dx.doi.org/10.1099/mic.0.029496-0.

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The phosphoenolpyruvate : carbohydrate phosphotransferase system (PTS) catalyses carbohydrate transport by coupling it to phosphorylation. Previously, we reported a Corynebacterium glutamicum R β-glucoside PTS encoded by bglF. Here we report that C. glutamicum R contains an additional β-glucoside PTS gene, bglF2, organized in a cluster with a putative phospho-β-glucosidase gene, bglA2, and a putative antiterminator, bglG2. While single gene disruption strains of either bglF or bglF2 were able to utilize salicin or arbutin as sole carbon sources, a double disruption strain exhibited defects in utilization of both carbon sources. Expression of both bglF and bglF2 was induced in the presence of either salicin or arbutin, although disruption of bglG2 affected only bglF2 expression. Moreover, in the presence of either salicin or arbutin, glucose completely repressed the expression of bglF but only slightly repressed that of bglF2. We conclude that BglF and BglF2 have a redundant role in β-glucoside transport even though the catabolite repression control of their encoding genes is different. We also show that expression of both bglF and bglF2 requires the general PTS.

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Erni, Bernhard. "The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction." Journal of the Iranian Chemical Society 10, no. 3 (December 18, 2012): 593–630. http://dx.doi.org/10.1007/s13738-012-0185-1.

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47

Zeng, G. Q., H. De Reuse, and A. Danchin. "Mutational analysis of the enzyme IIIGlc of the phosphoenolpyruvate phosphotransferase system in Escherichia coli." Research in Microbiology 143, no. 3 (January 1992): 251–61. http://dx.doi.org/10.1016/0923-2508(92)90017-i.

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48

Jamal, Zohra, Cécile Miot-Sertier, François Thibau, Lucie Dutilh, Aline Lonvaud-Funel, Patricia Ballestra, Claire Le Marrec, and Marguerite Dols-Lafargue. "Distribution and Functions of Phosphotransferase System Genes in the Genome of the Lactic Acid Bacterium Oenococcus oeni." Applied and Environmental Microbiology 79, no. 11 (March 22, 2013): 3371–79. http://dx.doi.org/10.1128/aem.00380-13.

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ABSTRACTOenococcus oeni, the lactic acid bacterium primarily responsible for malolactic fermentation in wine, is able to grow on a large variety of carbohydrates, but the pathways by which substrates are transported and phosphorylated in this species have been poorly studied. We show that the genes encoding the general phosphotransferase proteins, enzyme I (EI) and histidine protein (HPr), as well as 21 permease genes (3 isolated ones and 18 clustered into 6 distinct loci), are highly conserved among the strains studied and may form part of theO. oenicore genome. Additional permease genes differentiate the strains and may have been acquired or lost by horizontal gene transfer events. The coreptsgenes are expressed, and permease gene expression is modulated by the nature of the bacterial growth substrate. DecryptifiedO. oenicells are able to phosphorylate glucose, cellobiose, trehalose, and mannose at the expense of phosphoenolpyruvate. These substrates are present at low concentrations in wine at the end of alcoholic fermentation. The phosphotransferase system (PTS) may contribute to the perfect adaptation ofO. oenito its singular ecological niche.

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LOLKEMA, Juke S., Ria H. TEN HOEVE-DUURKENS, and George T. ROBILLARD. "The phosphoenolpyruvate-dependent fructose-specific phosphotransferase system in Rhodopseudomonas sphaeroides. Mechanism for transfer of the phosphoryl group from phosphoenolpyruvate to fructose." European Journal of Biochemistry 149, no. 3 (June 1985): 625–31. http://dx.doi.org/10.1111/j.1432-1033.1985.tb08970.x.

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50

Veyrat, A., M. J. Gosalbes, and G. Perez-Martinez. "Lactobacillus curvatus has a glucose transport system homologous to the mannose family of phosphoenolpyruvate-dependent phosphotransferase systems." Microbiology 142, no. 12 (December 1, 1996): 3469–77. http://dx.doi.org/10.1099/13500872-142-12-3469.

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