Phosphotransferase system and

H189E <1> (<1> comparable to wild type enzyme [26] <1> thermodynamics [29] <1> mutant retains ability for phosphorylation [34]) [26, 29, 34] Additional information <1, 3, 6, 12> (<1,3,6> overview on mutants [19] <1> N-terminal domain, thermodynamic properties [25,29] <3,6,12> enzyme deletion mutants, virulence of [31] <6> enzyme deletion mutant, alternative pathways [36] <1> fusion protein of enzyme plus the remaining three subunits of glucose phosphotransferase system and Ala-Pro-rich linker sequences [32]) [19, 25, 29, 31, 32]... 

Alice, A.E Perez-Martinez, G. Sanchez-Rivas, C. Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine metabolism in Bacillus sphaericus. Microbiology, 149, 1687-1698 (2003)... 

Chassy, B. M. and Thompson, J. 1983. Regulation of lactose-phosphoenolpyruvate-dependent phosphotransferase system and 0-D-phosphogalactoside galactohydrol-ase activities in Lactobacillus casei. J. Bacteriol 154, 1195-1203. 

Roseman, S. 1972. A bacterial phosphotransferase system and its role in sugar transport. In The Molecular Basis of Biological Transport. J. F. Woissner, Jr. and J. Huijing (Editors). Academic Press, New York, pp. 181-218. 

Much of the work defining the galactoside permease systems of E. coli was done before the discovery of the ubiquitous phosphotransferases of bacteria. There is now much discussion as to the relative importance of the permease and phosphotransferase systems and on the possible re-interpretation of some of the models proposed for permease systems, because of the new information on the phosphotransferases. 

Alditols are often observed as the end-products of monosaccharide metabolism that are stored in various cellular and tissue compartments with low redox potentials. However, there are also examples of alditols as important metabolic intermediates allowing the interconversion of rare forms of certain monosaccharides. In enteric bacteria such as Escherichia coli the hexitol galactitol is taken up through enzyme II of the phosphoenol pyruvate-dependent phosphotransferase system and accumulated inside the cell as galactitol 1-phosphate. The genes involved in galactitol metabolism have been cloned on a 7.8 kb DNA fragment [201]. 

Several novel 5-substituted A -hydroxy-2 -deoxycytidine 5 -phosphates (24) with substituents of different electronic, hydrophobic and steric properties at the 5-position were synthesised chemoenzymatically with the aid of the wheat shoot phosphotransferase system and evaluated as putative inhibitors of thymidylate synthase. All A -hydroxy-dCMP (24a) and dUMP analogues (24b) were competitive inhibitors of the enzyme-catalysed dUMP methylation. The inhibitory activity was attributed to the rare ram-rotamer (A/ -OH pointing towards C5), and therefore weaker slow-binding inhibitors were detected when unfavourable 04-C5-substituent steric interactions were present. 

Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC. J. Bacterial. 180, 4475- 480. 

Lux, R., Jahreis, K., Bettenbrock, K., Parkinson, J.S. and Lengeler, J.W. (1995). Couphng the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 92, 11583-11587. 

Mori, M. and Shiio, I. (1987) Phospho-enolpyruvatei sugar phosphotransferase systems and sugar metabolism in... 

FIGURE 10.26 Glucose transport in E. coli is mediated by the PEP-dependent phosphotransferase system. Enzyme I is phosphorylated in the first step by PEP. Successive phosphoryl transfers to HPr and Enzyme III in Steps 2 and 3 are followed by transport and phosphorylation of glucose. Enzyme II is the sugar transport channel. 

In this chapter, we have examined coupled transport systems that rely on ATP hydrolysis, on primary gradients of Na or Ff, and on phosphotransferase systems. Suppose you have just discovered an unusual strain of bacteria that transports rhamnose across its plasma membrane. Suggest experiments that would test whether it was linked to any of these other transport systems. 

Meadow, N. D., Fox, D. K., and Roseman, S., 1990. The bacterial phos-phoenolpyrnvate glycose phosphotransferase system. Annual Review of Biochemistry 59 497-542. 

The Enzymes II (E-IIs) of the phosphoenolpyruvate (P-enolpyruvate)-dependent phosphotransferase system (PTS) are carbohydrate transporters found only in prokaryotes. They not only transport hexoses and hexitols, but also pentitols and disaccharides. The PTS substrates are listed in Table I. The abbreviations used (as superscripts) throughout the text for these substrates are as follows Bgl, jS-gluco-side Cel, cellobiose Fru, fructose Glc, glucose Gut, glucitol Lac, lactose Man, mannose Mtl, mannitol Nag, iV-acetylglucosamine Scr, sucrose Sor, sorbose Xtl, xylitol. 

The bacterial phosphoenolpyruvate (PEP)-dependent carbohydrate phosphotransferase systems (PTS) are characterised by their unique mechanism of group translocation. The transported solute is chemically modified (i.e. phos-phorylated) during the process (for comprehensive reviews see [151,152] and... 

Hardesty, C., Ferran, C. and DiRienzo, J. M. (1991). Plasmid-mediated sucrose metabolism in Escherichia colt characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin, J. Bacteriol, 173, 449-456. 

Siebold, C., Flukiger, K., Beutler, R. and Emi, B. (2001). Carbohydrate transporters of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS), FEBS Lett. 504, 104-111. 

Kohlbrecher, D. Eisermann, R. Hengstenberg, W. Staphylococcal phos-phoenolpyruvate-dependent phosphotransferase system molecular cloning and nucleotide sequence of the Staphylococcus carnosus ptsi gene and expression and complementation studies of the gene product. J. Bacteriol., 174, 2208-2214 (1992)... 

Weigel, N. Waygood, E.B. Kukuruzinska, M.A. Nakazawa, A. Roseman, S. Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of enzyme I from Salmonella typhimurium. J. Biol. Chem., 257, 14461-14469 (1982)... 

Hoving, H. Koning, J.H. Robillard, G.T. Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system role of divalent metals in the dimerization and phosphorylation of enzyme I. Biochemistry, 21, 3128-3136 (1982)... 

Durham, D.R. Phibbs, P.V. Fractionation and characterization of the phos-phoenolpyruvate fructose 1-phosphotransferase system from Pseudomonas aeruginosa. J. Bacteriol., 149, 534-541 (1982)... 

Waygood, E.B. Sleeves, T. Enzyme I of the phosphoenolpyruvate sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties. Can. J. Biochem., 58, 40-48 (1980)... 

Jaffor Ullah, A.H. Cirillo, V.P. Mycoplasma phosphoenolpyruvate-depen-dent sugar phosphotransferase system purification and characterization of enzyme I. J. Bacteriol., 131, 988-996 (1977)... 

De Reuse, H. Danchin, A. The ptsH, ptsI, and err genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system a complex operon with several modes of transcription. J. Bacteriol., 170, 3827-3837 (1988)... 

Chauvin, F. Fomenkov, A. Johnson, C.R. Roseman, S. The N-terminal domain of Escherichia coli enzyme I of the phosphoenolpyruvate/glycose phosphotransferase system molecular cloning and characterization. Proc. Natl. Acad. Sci.USA, 93, 7028-7031 (1996)... 

Huebner, G. Koenig, S. Koch, M.H.J. Hengstenberg, W. Influence of Phosphoenolpyruvate and Magnesium Ions on the Quaternary Structure of Enzyme I of the Phosphotransferase System from Gram-Positive Bacteria. Biochemistry, 34, 15700-15703 (1995)... 

Mao, Q. Schunk, T. Gerber, B. Erni, B. A string of enzymes, purification and characterization of a fusion protein comprising the four subunits of the glucose phosphotransferase system of Escherichia coli. J. Biol. Chem., 270, 18295-18300 (1995)... 

Napper, S. Delbaere, L.T.J. Waygood, E.B. The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli phosphoenolpyruvate sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization. J. Biol. Chem., 274, 21776-21782 (1999)... 

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