An Inducible Phosphoenolpyruvate: Dihydroxyacetone Phosphotransferase System in Escherichia coli

Jin, Ruzhong; Lin, E. C. C.

doi:10.1099/00221287-130-1-83

Cited by 34 publications

(39 citation statements)

References 20 publications

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“…Thus, DhaH is a functional PTS protein, but it is not capable of self-phosphorylation in the absence of other PTS proteins, presumably because it lacks the C-terminal PEP-binding\catalytic domain of Enzyme I. This latter observation is consistent with the results of Jin & Lin (4) suggesting that DHA phosphorylation is dependent on Enzyme I of the PTS.…”

Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Isupporting

confidence: 81%

“…These observations contrast with the earlier report of Jin & Lin (4) suggesting that the PTS is responsible for phosphorylation of DHA. Indeed the region implicated in DHA utilization lacks any apparent Enzyme II of the PTS.…”

Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Icontrasting

confidence: 56%

“…In an early report, several lines of evidence suggested that a DHAinduced phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) was responsible for the uptake and phosphorylation of DHA in E. coli (4). First, using a spectrophotometric assay, PEP was converted to pyruvate in the presence of DHA.…”

Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Imentioning

confidence: 99%

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Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

et al. 2000

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Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Isupporting

confidence: 81%

Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Icontrasting

confidence: 56%

Section: Functional Genomic Studies Of Dihydroxyacetone Utilization Imentioning

confidence: 99%

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Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

et al. 2000

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“…Although several bacteria metabolize dihydroxyacetone via ATP-dependent phosphorylation, a PEPdependent pathway is operative in E. coli (376). Mutations in ptsI or the dha operon abolish phosphorylation of dihydroxyacetone and thereby growth on this carbon source.…”

Section: Pep-dependent Dihydroxyacetone Phosphorylationmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,187

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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“…Nonetheless, a triply mutated E. coli can convert glycerol to dihydroxyacetone, which is initially excreted and subsequently metabolized (152). Furthermore, wild-type E. coli can use dihydroxyacetone as the sole carbon source (as long as the phosphate concentration is kept low) (86). Dihydroxyacetone kinase has yet to be assayed from E. coli.…”

Section: -Dependent Activatorsmentioning

confidence: 99%

Metabolic Context and Possible Physiological Themes of ς⁵⁴-Dependent Genes inEscherichia coli

Reitzer

Schneider

2001

Microbiol Mol Biol Rev

250

300

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SUMMARY ς54 has several features that distinguish it from other sigma factors in Escherichia coli: it is not homologous to other ς subunits, ς54-dependent expression absolutely requires an activator, and the activator binding sites can be far from the transcription start site. A rationale for these properties has not been readily apparent, in part because of an inability to assign a common physiological function for ς54-dependent genes. Surveys of ς54-dependent genes from a variety of organisms suggest that the products of these genes are often involved in nitrogen assimilation; however, many are not. Such broad surveys inevitably remove the ς54-dependent genes from a potentially coherent metabolic context. To address this concern, we consider the function and metabolic context of ς54-dependent genes primarily from a single organism, Escherichia coli, in which a reasonably complete list of ς54-dependent genes has been identified by computer analysis combined with a DNA microarray analysis of nitrogen limitation-induced genes. E. coli appears to have approximately 30 ς54-dependent operons, and about half are involved in nitrogen assimilation and metabolism. A possible physiological relationship between ς54-dependent genes may be based on the fact that nitrogen assimilation consumes energy and intermediates of central metabolism. The products of the ς54-dependent genes that are not involved in nitrogen metabolism may prevent depletion of metabolites and energy resources in certain environments or partially neutralize adverse conditions. Such a relationship may limit the number of physiological themes of ς54-dependent genes within a single organism and may partially account for the unique features of ς54 and ς54-dependent gene expression.

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An Inducible Phosphoenolpyruvate: Dihydroxyacetone Phosphotransferase System in Escherichia coli

Cited by 34 publications

References 20 publications

Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Metabolic Context and Possible Physiological Themes of ς⁵⁴-Dependent Genes inEscherichia coli

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An Inducible Phosphoenolpyruvate: Dihydroxyacetone Phosphotransferase System in Escherichia coli

Cited by 34 publications

References 20 publications

Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

Functional genomic studies of dihydroxyacetone utilization in Escherichia coli

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Metabolic Context and Possible Physiological Themes of ς54-Dependent Genes inEscherichia coli

Contact Info

Product

Resources

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Metabolic Context and Possible Physiological Themes of ς⁵⁴-Dependent Genes inEscherichia coli