Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria

Postma, P.; Lengeler, Joseph W.

doi:10.1128/mr.49.3.232-269.1985

Cited by 238 publications

(28 citation statements)

References 360 publications

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“…Following chitin utilization or autolytic cell-wall degradation, N-acetylglucosamine can enter the cell via at least three different sugar transporters, namely as the monomer via the NagE2 permease (SCO2907), which is part of the PTS phosphotransferase system, or as the dimer chitobiose via DasABC (SCO5232-5234), or via the NgcEFG transporter (SCO6005-6007) (Nothaft et al, 2003;Parche et al, 2000;Saito et al, 2007;Schlösser et al, 1999). The PTS consists of several carbohydrate-specific permeases (designated Enzyme IIBC) and a global part consisting of Enzyme I (EI, encoded by ptsI ), HPr (histidine protein, encoded by ptsH ), and Enzyme IIA (EIIA, encoded by crr) (Parche et al, 2000;Postma et al, 1993;Titgemeyer et al, 1995). EI, HPr, and EIIA form the phosphate-transfer system, using phosphoenolpyruvate as the energy source, resulting in phosphorylation of the incoming sugar.…”

Section: Interactions Between Metabolism and The Dasr Regulonmentioning

confidence: 99%

Chapter 5 Applying the Genetics of Secondary Metabolism in Model Actinomycetes to the Discovery of New Antibiotics

Wezel

McKenzie

Nodwell

2009

Methods in Enzymology

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The actinomycetes, including in particular members of the filamentous genus Streptomyces, are the industrial source of a large number of bioactive small molecules employed as antibiotics and other drugs. They produce these molecules as part of their "secondary" or nonessential metabolism. The number and diversity of secondary metabolic pathways is enormous, with some estimates suggesting that this one genus can produce more than 100,000 distinct molecules. However, the discovery of new antimicrobials is hampered by the fact that many wild isolates fail to express all or sometimes any of their secondary metabolites under laboratory conditions. Furthermore, the use of previously successful screening strategies frequently results in the rediscovery of known molecules: the all-important novel structures have proven to be elusive. Mounting evidence suggests that streptomycetes possess many regulatory pathways that control the biosynthetic gene clusters for these secondary metabolic pathways and that cell metabolism plays a significant role in limiting or potentiating expression as well. In this article we explore the idea that manipulating metabolic conditions and regulatory pathways can "awaken" silent gene clusters and lead to the discovery of novel antimicrobial activities.

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Section: Interactions Between Metabolism and The Dasr Regulonmentioning

confidence: 99%

Chapter 5 Applying the Genetics of Secondary Metabolism in Model Actinomycetes to the Discovery of New Antibiotics

Wezel

McKenzie

Nodwell

2009

Methods in Enzymology

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“…For most oral streptococci, carbohydrates are primarily internalized via the phosphoenolpyruvate::sugar phosphotransferase system (PTS), which is composed of two general proteins, Enzyme I (EI) and the phospho-carrier protein HPr, and a variety of carbohydrate-specific Enzymes II (EII) that are membraneassociated permeases (9). The PTS concurrently internalizes and phosphorylates carbohydrates that can be fed into the Embden-Meyerhoff-Parnas (EMP) pathway, which primarily yields pyruvate and the energy molecules ATP and NADH.…”

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confidence: 99%

Spontaneous Mutants of Streptococcus sanguinis with Defects in the Glucose-PTS Show Enhanced Post-Exponential Phase Fitness

Zeng

Walker

Lee

et al. 2021

Preprint

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Genetic truncations in a gene encoding a putative glucose-PTS protein (manL, EIIABMan) were identified in subpopulations of two separate laboratory stocks of Streptococcus sanguinis SK36; the mutants had reduced PTS activities on glucose and other monosaccharides. Using an engineered mutant of manL and its complemented derivative, we showed that the ManL-deficient strain had improved bacterial viability in stationary phase and was better able to inhibit the growth of the dental caries pathogen Streptococcus mutans. Transcriptional analysis and biochemical assays suggested that the manL mutant underwent reprograming of central carbon metabolism that directed pyruvate away from production of lactate, increasing production of hydrogen peroxide (H2O2) and excretion of pyruvate. Addition of pyruvate to the medium enhanced the survival of SK36 in overnight cultures. Meanwhile, elevated pyruvate levels were detected in the cultures of a small, but significant percentage (~10%), of clinical isolates of oral commensal bacteria. Furthermore, the manL mutant showed higher expression of the arginine deiminase system than the wild type, which enhanced the ability of the mutant to raise environmental pH when arginine was present. Significant discrepancies in genome sequence were identified between strain SK36 obtained from ATCC and the sequence deposited in GenBank. As the conditions that are likely associated with the emergence of spontaneous manL mutations, i.e. excess carbohydrates and low pH, are those associated with caries development, we propose that the glucose-PTS strongly influences commensal-pathogen interactions by altering the production of ammonia, pyruvate, and H2O2.

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“…led to the hypothesis that these domains, and possibly all pts molecules, share a common evolutionary origin (Lengeler & Steinberger 1978;Saier 1985; further references in Postma & Lengeler (1985)).…”

Section: Co P H O S P H O T R a N S F E R A S E Sy St Em P R O T E In Smentioning

confidence: 99%

“…[ 149 ] (pts) . It is the major transport system for many so-called PTS-carbohydrates that are phosphorylated concomitantly with the translocation of the substrate through the membrane (group translocation) (for recent reviews see Postma & Lengeler (1985); Saier (1985); Robillard & Lolkema (1988). The carbohydrate phosphate is the first intermediate in subsequent catabolism, thus providing a tight linkage between uptake and metabolism.…”

Section: T He C a R B O H Y D R A T E : P H O Sph O T R A N Sfe R A Se System (Pts)mentioning

confidence: 99%

Structures and homologies of carbohydrate: phosphotransferase system (PTS) proteins

Lengeler

Titgemeyer

Vogler

et al. 1990

Phil. Trans. R. Soc. Lond. B

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The bacterial phosphotransferase system (PTS) is the major transport system for many carbohydrates that are phosphorylated concomitantly with the translocation step through the membrane (group translocation). It consists of two general proteins, enzyme I and histidine protein (HPr), and a series of more than 15 substrate-specific enzymes II (EII). The sequences of several of these derived from Gram-positive and Gram-negative bacteria were compared, which allowed the possible identification of the following functional domains: membrane-bound pore, substrate-binding site, linker domains, transphosphorylation domain and primary phosphorylation site. Several EIIs have been analysed in the meantime, also by topological tests, by sequential deletion of the corresponding structural genes, and by construction of intergenic hybrids between different domains of several EIIs. These data suggest evolutionary relationships between different EIIs; they also enable a general model to be constructed of EIIs as carbohydrate transport systems, phosphotransferases, chemoreceptors in chemotaxis and as part of a global regulatory network.

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Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria

Cited by 238 publications

References 360 publications

Chapter 5 Applying the Genetics of Secondary Metabolism in Model Actinomycetes to the Discovery of New Antibiotics

Chapter 5 Applying the Genetics of Secondary Metabolism in Model Actinomycetes to the Discovery of New Antibiotics

Spontaneous Mutants of Streptococcus sanguinis with Defects in the Glucose-PTS Show Enhanced Post-Exponential Phase Fitness

Structures and homologies of carbohydrate: phosphotransferase system (PTS) proteins

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