Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria

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Published in	Microbiological Reviews Vol. 57; no. 3; pp. 543 - 594
Main Authors	Postma, P W, Lengeler, J W, Jacobson, G R
Format	Journal Article
Language	English
Published	Washington, DC American Society for Microbiology 01.09.1993
Subjects	Adenylyl Cyclases - metabolism Amino Acid Sequence Bacteria Bacteria - genetics Bacteria - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Biological Transport Carbohydrate Metabolism Carbohydrates Chemotaxis Cyclic AMP - physiology Energy Metabolism Enzymes Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Genes, Bacterial Metabolism. Enzymes Microbiology Molecular Sequence Data Operon Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry Phosphoenolpyruvate Sugar Phosphotransferase System - classification Phosphoenolpyruvate Sugar Phosphotransferase System - genetics Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Phosphorylation Protein Conformation Signal Transduction Species Specificity Proteins Gene Enzyme Membrane transport Bacteria Carbohydrate Review Gene expression Phosphoenolpyruvate-dependent phosphotransferase system Uptake
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Abstract	Article Usage Stats Services MMBR Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue MMBR About MMBR Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MMBR RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1092-2172 Online ISSN: 1098-5557 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MMBR .asm.org, visit: MMBR
AbstractList	Article Usage Stats Services MMBR Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue MMBR About MMBR Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MMBR RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1092-2172 Online ISSN: 1098-5557 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MMBR .asm.org, visit: MMBR Numerous gram-negative and gram-positive bacteria take up carbohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). This system transports and phosphorylates carbohydrates at the expense of PEP and is the subject of this review. The PTS consists of two general proteins, enzyme I and HPr, and a number of carbohydrate-specific enzymes, the enzymes II. PTS proteins are phosphoproteins in which the phospho group is attached to either a histidine residue or, in a number of cases, a cysteine residue. After phosphorylation of enzyme I by PEP, the phospho group is transferred to HPr. The enzymes II are required for the transport of the carbohydrates across the membrane and the transfer of the phospho group from phospho-HPr to the carbohydrates. Biochemical, structural, and molecular genetic studies have shown that the various enzymes II have the same basic structure. Each enzyme II consists of domains for specific functions, e.g., binding of the carbohydrate or phosphorylation. Each enzyme II complex can consist of one to four different polypeptides. The enzymes II can be placed into at least four classes on the basis of sequence similarity. The genetics of the PTS is complex, and the expression of PTS proteins is intricately regulated because of the central roles of these proteins in nutrient acquisition. In addition to classical induction-repression mechanisms involving repressor and activator proteins, other types of regulation, such as antitermination, have been observed in some PTSs. Apart from their role in carbohydrate transport, PTS proteins are involved in chemotaxis toward PTS carbohydrates. Furthermore, the IIAGlc protein, part of the glucose-specific PTS, is a central regulatory protein which in its nonphosphorylated form can bind to and inhibit several non-PTS uptake systems and thus prevent entry of inducers. In its phosphorylated form, P-IIAGlc is involved in the activation of adenylate cyclase and thus in the regulation of gene expression. By sensing the presence of PTS carbohydrates in the medium and adjusting the phosphorylation state of IIAGlc, cells can adapt quickly to changing conditions in the environment. In gram-positive bacteria, it has been demonstrated that HPr can be phosphorylated by ATP on a serine residue and this modification may perform a regulatory function. Numerous gram-negative and gram-positive bacteria take up carbohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). This system transports and phosphorylates carbohydrates at the expense of PEP and is the subject of this review. The PTS consists of two general proteins, enzyme I and HPr, and a number of carbohydrate-specific enzymes, the enzymes II. PTS proteins are phosphoproteins in which the phospho group is attached to either a histidine residue or, in a number of cases, a cysteine residue. After phosphorylation of enzyme I by PEP, the phospho group is transferred to HPr. The enzymes II are required for the transport of the carbohydrates across the membrane and the transfer of the phospho group from phospho-HPr to the carbohydrates. Biochemical, structural, and molecular genetic studies have shown that the various enzymes II have the same basic structure. Each enzyme II consists of domains for specific functions, e.g., binding of the carbohydrate or phosphorylation. Each enzyme II complex can consist of one to four different polypeptides. The enzymes II can be placed into at least four classes on the basis of sequence similarity. The genetics of the PTS is complex, and the expression of PTS proteins is intricately regulated because of the central roles of these proteins in nutrient acquisition. In addition to classical induction-repression mechanisms involving repressor and activator proteins, other types of regulation, such as antitermination, have been observed in some PTSs. Apart from their role in carbohydrate transport, PTS proteins are involved in chemotaxis toward PTS carbohydrates. Furthermore, the IIA super(Glc) protein, part of the glucose-specific PTS, is a central regulatory protein which in its nonphosphorylated form can bind to and inhibit several non-PTS uptake systems and thus prevent entry of inducers. In its phosphorylated form, P-IIA super(Glc) is involved in the activation of adenylate cyclase and thus in the regulation of gene expression. By sensing the presence of PTS carbohydrates in the medium and adjusting the phosphorylation state of IIA super(Glc), cells can adapt quickly to changing conditions in the environment. In gram-positive bacteria, it has been demonstrated that HPr can be phosphorylated by ATP on a serine residue and this modification may perform a regulatory function. Numerous gram-negative and gram-positive bacteria take up cabrohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system. This system, which transports and phosphorylates carbohydrates at the expense of PEP, is examined.
Author	P W Postma G R Jacobson J W Lengeler
AuthorAffiliation	E. C. Slater Institute, University of Amsterdam, The Netherlands
AuthorAffiliation_xml	– name: E. C. Slater Institute, University of Amsterdam, The Netherlands
Author_xml	– sequence: 1 givenname: P W surname: Postma fullname: Postma, P W – sequence: 2 givenname: J W surname: Lengeler fullname: Lengeler, J W – sequence: 3 givenname: G R surname: Jacobson fullname: Jacobson, G R
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3777585$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/8246840$$D View this record in MEDLINE/PubMed
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Snippet	Article Usage Stats Services MMBR Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... Numerous gram-negative and gram-positive bacteria take up carbohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS).... Numerous gram-negative and gram-positive bacteria take up cabrohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system. This...
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SubjectTerms	Adenylyl Cyclases - metabolism Amino Acid Sequence Bacteria Bacteria - genetics Bacteria - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Biological Transport Carbohydrate Metabolism Carbohydrates Chemotaxis Cyclic AMP - physiology Energy Metabolism Enzymes Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Genes, Bacterial Metabolism. Enzymes Microbiology Molecular Sequence Data Operon Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry Phosphoenolpyruvate Sugar Phosphotransferase System - classification Phosphoenolpyruvate Sugar Phosphotransferase System - genetics Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Phosphorylation Protein Conformation Signal Transduction Species Specificity
Title	Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
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