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Опубліковано: 6 вересня 2023

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Статті в журналах з теми "Phosphoenolpyruvate -phosphotransferase system"

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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Анотація:
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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Анотація:
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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Більше джерел

Дисертації з теми "Phosphoenolpyruvate -phosphotransferase system"

1

Thevenot, Tracy Lynn. "Aspects of sugar transport via the phosphoenolpyruvate sugar phosphotransferase system of streptococcus mutans /." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq23673.pdf.

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2

Sliz, Piotr. "Structure, function and interactions of enzyme IIA from the phosphoenolpyruvate, lactose phosphotransferase system." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0020/NQ53658.pdf.

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3

Thapar, Roopa. "Heteronuclear NMR studies on mutants of HPr from Escherichia coli /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/9218.

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4

Macfadyen, Leah Pauline. "Regulation of intracellular cAMP levels and competence development in Haemophilus influenza by a phosphoenolpyruvate, fructose phosphotransferase system." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0019/NQ46381.pdf.

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5

Kiel, Kathrin. "Einfluss des Phosphoenolpyruvat-Zucker-Phosphotransferase-Systems auf die Expression des interzellulären Polysaccharid-Adhäsins von mukoiden Staphylococcus epidermidis." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964294052.

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6

Levy, Sophie. "Construction et etude de souches de escherichia coli k 12 portant une deletion pour les genes ptsh ptsi et crr du systeme des phosphotransferases dependantes du phosphoenolpyruvate (pts)." Paris 7, 1987. http://www.theses.fr/1987PA077221.

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Анотація:
Le systeme des phosphotransferases dependant du phosphoenol pyruvate (pts) d'escherichia coli regule l'utilisation par la cellule de nombreuses sauces de carbone. Pour preciser le role des differentes proteines du pts dans cette regulation; et dans la modulation de la synthese amp cyclique, 5 souches isogeniques portant differentes deletions dans l'operon pts parfaitement delimites ont ete construites. Ces souches presentent un phenotype maltose**(-). Une mutation supplementaire, obtenue par l'introduction d'un transposon sur le chromosome d'une souche deletee pour l'operon pts restante un phenotype maltose**(+) en augmentant le taux ampc. Cette mutation revele l'existence d'un facteur regulateur de la synthese ou l'activite de l'adenylate cyclase, jusqu'ici
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7

Lin, Shih-Hong, and 林世浤. "Virtual Screening for the PTSI (the phosphoenolpyruvate: sugar phosphotransferase system enzyme I) Inhibitors." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/22981889952706911831.

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碩士
國立東華大學
生物技術研究所
97
The PTS system (phosphoenolpyruvate: sugar phosphotransferase system ), mediates the phosphorylation of sugar, is one of the most common important metabolic pathways of bacteria. The present study for use on screening though computer virtual screening bacterial PTSI (EI) inhibitors, the as a potential development of new generation antibiotics. First, we obrained, 1ZYM, the 3D structure of N-domain of PTSI as the receptor molecular from the drug-like subset of database, we filtered out of 29,169 small molecular band on physico-chemical characteristics. Then we used IDDS (Integrated Drug Design System) software to select509 small molecules with lower energy. More sophisticated virtual screening we perform using DS (Discovery Studio) software obtained the final hert 10 ligands. Protein-ligand interaction analysis indicated that: the ligands with 1ZYM and for meed H-bond with residues Glu125, Asp129, Asp162, which are part of the active site of PTSI which contains Glu68, Glu121, Glu125, Asp129, Asp132, Asp162, Glu167 and His189。
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8

Macfadyen, Leah Pauline. "Regulation of intracellular cAMP levels and competence development in haemophilus influenzae by a phosphoenolpyruvate : fructose phosphotransferase system." Thesis, 1999. http://hdl.handle.net/2429/10013.

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Diverse and distantly-related bacteria can develop competence for natural transformation. Competent cells can bind free extracellular DNA, transport it into the cytoplasm, and sometimes recombine it into the chromosome. Competence has a long evolutionary history and is therefore expected to significantly benefit the cell. In an attempt to elucidate the function (benefit) of natural competence, I have carried out genetic studies of the regulation of competence development in Haemophilus influenzae. Competence in this organism is dependent on an increase in intracellular concentrations of cAMP complexed with its receptor, CRP. In related bacteria, cAMP synthesis by adenylate cyclase is regulated in response to carbon source availability by the phosphoenolpyruvate:glycose phosphotransferase system (PTS). This enzyme complex detects availability of preferred sugars, and transports them into the cell. In the absence of preferred sugars, the PTS activates adenylate cyclase. I demonstrated the existence of a simple fructose-specific PTS in H. influenzae by cloning the pts and fru operons. I disrupted genes encoding PTS components, constructed mutant strains, and assessed the effect of these mutations on competence and other cAMP-dependent phenotypes. Strains lacking or unable to activate the putative adenylate cyclase-regulating component of this PTS (EIIA[sup Glc]) showed a 150-fold reduction in competence under standard competence-inducing conditions, unless exogenous cAMP was added. Moreover, these PTS-deficient strains could not catabolize cAMP-dependent sugars, and showed reduced (3- galactosidase expression from a cAMP-dependent /acZ-based reporter construct, implying that the H. influenzae regulates adenylate cyclase activity and competence. Competence was also found to be optimized by a cAMP-phosphodiesterase and reduced by the presence of physiological concentrations of free nucleotides. Putative regulatory sites in the promoters of competence genes were shown to be indistinguishable from cAMP-CRP binding sites, suggesting that the cAMP-CRP complex regulates transcription of these genes. In conclusion, adenylate cyclase activity and competence in H. influenzae are regulated by nutritional signals. It is proposed that cells may therefore transport DNA for the nucleotides it contains, and that competence may be part of the hunger response of H. influenzae and other bacteria to nutritional stress.
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9

Kiel, Kathrin [Verfasser]. "Einfluss des Phosphoenolpyruvat-Zucker-Phosphotransferase-Systems auf die Expression des interzellulären Polysaccharid-Adhäsins von mukoiden Staphylococcus epidermidis / vorgelegt von Kathrin Kiel." 2002. http://d-nb.info/964294052/34.

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Книги з теми "Phosphoenolpyruvate -phosphotransferase system"

1

Sliz, Piotr. Structure, function and interactions of enzyme IIA from the phosphoenolpyruvate: Lactose phosphotransferase system. 2000.

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Частини книг з теми "Phosphoenolpyruvate -phosphotransferase system"

1

Roseman, Saul. "The Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System." In Ciba Foundation Symposium 31 - Energy Transformation in Biological Systems, 225–41. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720134.ch13.

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2

Jeckelmann, Jean-Marc, and Bernhard Erni. "Carbohydrate Transport by Group Translocation: The Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System." In Subcellular Biochemistry, 223–74. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-18768-2_8.

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3

Postma, Pieter W. "The Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System of Escherichia coli and Salmonella typhimurium." In Carbohydrate Metabolism in Cultured Cells, 357–408. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-7679-8_10.

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4

Lengeler, Joseph W. "The Phosphoenolpyruvate-Dependent Carbohydrate: Phosphotransferase System (PTS) and Control of Carbon Source Utilization." In Regulation of Gene Expression in Escherichia coli, 231–54. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4684-8601-8_11.

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5

Saier, Milton H. "Group Translocation Catalyzed by the Phosphoenolpyruvate: Sugar Phosphotransferase System." In Mechanisms and Regulation of Carbohydrate Transport in Bacteria, 49–79. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-614780-3.50009-0.

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