Literature DB >> 3060316

The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation.

J Reizer1, M H Saier, J Deutscher, F Grenier, J Thompson, W Hengstenberg.   

Abstract

This review consists of three major sections. The first and largest section reviews the protein constituents and known properties of the phosphotransferase systems present in well-studied Gram-positive bacteria. These bacteria include species of the following genera: (1) Staphylococcus, (2) Streptococcus, (3) Bacillus, (4) Lactobacillus, (5) Clostridium, (6) Arthrobacter, and (7) Brochothrix. The properties of the different systems are compared. The second major section deals with the regulation of carbohydrate uptake. There are four parts: (1) inhibition by intracellular sugar phosphates in Staphylococcus aureus, (2) PTS-mediated regulation of glycerol uptake in Bacillus subtilis, (3) competition for phospho-HPr in Streptococcus mutans, and (4) the possible involvement of protein kinases in the regulation of sugar uptake via the phosphotransferase system. The third section deals with the phenomenon of inducer expulsion. The first part is concerned with the physiological characterization of the phenomenon; then the consequences of unregulated uptake and expulsion, a futile cycle of energy expenditure, are considered. Finally, the biochemistry of the protein kinase and the protein phosphate phosphatase system, which appears to regulate sugar transport via the phosphotransferase system, is defined. The review, therefore, concentrates on the phosphotransferase system, its functions in carbohydrate transport and phosphorylation, the mechanisms of its regulation, and the mechanism by which it participates in the regulation of other physiological processes in the bacterial cell.

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Year:  1988        PMID: 3060316     DOI: 10.3109/10408418809104461

Source DB:  PubMed          Journal:  Crit Rev Microbiol        ISSN: 1040-841X            Impact factor:   7.624


  49 in total

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3.  Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.

Authors:  M H Saier; J Reizer
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5.  Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr.

Authors:  S Sharma; F Georges; L T Delbaere; J S Lee; R E Klevit; E B Waygood
Journal:  Proc Natl Acad Sci U S A       Date:  1991-06-01       Impact factor: 11.205

6.  Regulation of sugar uptake via the phosphoenolpyruvate-dependent phosphotransferase systems in Bacillus subtilis and Lactococcus lactis is mediated by ATP-dependent phosphorylation of seryl residue 46 in HPr.

Authors:  J J Ye; M H Saier
Journal:  J Bacteriol       Date:  1996-06       Impact factor: 3.490

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8.  Glucose kinase-dependent catabolite repression in Staphylococcus xylosus.

Authors:  E Wagner; S Marcandier; O Egeter; J Deutscher; F Götz; R Brückner
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9.  Structural insights into the substrate specificity of a 6-phospho-β-glucosidase BglA-2 from Streptococcus pneumoniae TIGR4.

Authors:  Wei-Li Yu; Yong-Liang Jiang; Andreas Pikis; Wang Cheng; Xiao-Hui Bai; Yan-Min Ren; John Thompson; Cong-Zhao Zhou; Yuxing Chen
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10.  Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

Authors:  O Herzberg; P Reddy; S Sutrina; M H Saier; J Reizer; G Kapadia
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

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