Phosphoenolpyruvate-dependent

J. V. Rodriguez, J. A. Kaandorp, M. Dobrzynski, and J. K. Blom, Spatial stochastic modelling of the phosphoenolpyruvate-dependent phosphotransferase (PTS) pathway in Escherichia coli, Bioinformatics 22, 1895 (2006). 

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. 

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)... 

Robillard, G.T. Dooijewaard, G. Lolkema, J. Escherichia coli phosphoenolpyruvate dependent phosphotransferase system. Complete purification of enzyme I by hydrophobic interaction chromatography. Biochemistry, 18, 2984-2989 (1979)... 

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)... 

Enzymatic synthesis relying on the use of aldolases offers several advantages. As opposed to chemical aldolization, aldolases usually catalyze a stereoselective aldol reaction under mild conditions there is no need for protection of functional groups and no cofactors are required. Moreover, whereas high specificity is reported for the donor substrate, broad flexibility toward the acceptor is generally observed. Finally, aldolases herein discussed do not use phosphorylated substrates, contrary to phosphoenolpyruvate-dependent aldolases involved in vivo in the biosynthetic pathway, such as KDO synthetase or DAHP synthetase [18,19]. 

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. 

Park, Y. H. and McKay, L. L. 1982. Distinct galactose phosphoenolpyruvate-dependent phosphotransferase system in Streptococcus lactis. J. Bacterial 149, 420-425. 

Other pyruvate- and phosphoenolpyruvate-dependent aldolases have been isolated and purified, but have not yet been extensively investigated for synthetic use. Those showing promise for future applications include, 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate (DAHP) synthetase (EC 4.1.2.15), 2-keto-4-hydroxyglutarate (KHG) aldolase (EC 4.1.2.31), and 2-keto-3-deoxy-D-gluconate (KDG) aldolase (EC 4.1.2.20). DAHP synthetase has been used... 

The aldolases which have been investigated for their synthetic utility can be classified on the basis of the donor substrate accepted by the enzyme. For the synthesis of 3-deoxy-2-ulosonic acids pyruvate- and phosphoenolpyruvate dependent aldolases are the most desirable enzymes as they are involved in the metabolism of sialic acids (or structurally related ones) in vivo. They use pyruvate or phosphoenolpyruvate as a donor to form 3-deoxy-2-keto acids (Table 1). Both of them add a three-carbons ketone fragment onto a carbonyl group of an aldehyde. The pyruvate dependent aldolases have a catabolic function in vivo, whereas the phosphoenolpyruvate dependent aldolases are involved in the biosynthesis of the keto acids. For synthetic purpose the equilibrium of the pyruvate dependent aldolases is shifted toward the condensation products through the use of an excess of pyruvate. 

D-mannitol <2> (<2>, strong substrate inhibition at neutral pH in the transphosphorylation reaction. No substrate inhibition for phosphoenolpyruvate-dependent reaction [10]) [10, 32]... 

Additional information <2> (<2> antibodies directed against the enzyme inhibit phosphoenolpyruvate-dependent activity to a greater extent than the transphosphorylation [10]) [10]... 

Hiidig, H. Hengstenberg, W. The bacterial phosphoenolpyruvate dependent phosphotransferase system (PTS) solubilisation and kinetic para-... 

Peters, D. Frank, R. Hengstenberg, W. Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterization. Eur. J. Biochem., 228, 798-804 (1995)... 

Abbreviations Acs, acetyl coenzyme A synthetase CheA P, phosphorylated CheA CheY P, phosphorylated CheY FRET, fluorescence resonance energy transfer GFP, green-fluorescent protein PTS, phosphoenolpyruvate-dependent carbohydrate phosphotransferase system YFP, yellow-fluorescent protein. 

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. 

Lengeler, J., Auburger, A.-M., Mayer, R. and Pecher, A. (1981). The phosphoenolpyruvate-dependent carbohydrate Phosphotransferase system enzymes 11 as chemoreceptors in chemotaxis of Escherichia coli K12. Mol. Gen. Genet. 183, 163-170. 

Robfllard, G.T and Broos, J. (1999). Stmcture/fimction studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system. Biochim. Biophys. Acta 1422, 73—104. 

A soluble carrier protein (HPr), one of the common components of all phosphoenolpyruvate-dependent phosphotransferase systems, has been purified from the phosphoenolpyruvate-dependent phosphotransferase system of... 

For example, in order to produce polyhydroxybutyrate (PHB) from a mixture of xylose and glucose, Lee et al. knocked out the ptsG gene, which encoded a glucose-specific enzyme, in phosphoenolpyruvate-dependent glucose-specific PTS... 

Xiao H, Gu Y, NingY.YangY, Mitchell WJ, Jiang W, et al. Confirmation and elimination of xylose metabolism bottlenecks in glucose phosphoenolpyruvate-dependent phosphotransferase system-deficient Clostridium acetobutylicum for simultaneous utilization of glucose, xylose, and arabinose. Appl Environ Microbiol 2011 77 7886-95. 

The chemotactic receptors to glucose, fructose, mannose and certain other sugars are insensitive to osmotic shock (Table 4.1) and have been shown to be integral parts of the cytoplasmic membrane. These membrane-associated receptors have been shown to be identical with enzymes II, the substrate-specific components of phosphotransferase transport (the PEP system). The essential event during sugar translocation using the PEP system is the phosphoenolpyruvate-dependent phosphorylation of the... 

Pickl, A., Johnsen, U., and Schonheit, P. (2012) Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-l-phosphate kinase, and class 11 fructose-1,6-bisphosphate aldolase. J Bacteriol 194, 3088-3097. 

The pyruvate and phosphoenolpyruvate dependent aldolases are an important group of enzymes catalyzing the synthesis of a-oxoacids from a variety of polyhydroxylated aldehydes. They are usually type I aldolases. In vivo, the... 

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