PMID:11361069: Difference between revisions

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<span style = 'font-size: large'> '''Seok, YJ, Koo, BM, Sondej, M and Peterkofsky, A'''  (2001) Regulation of E. coli glycogen phosphorylase activity by HPr.''J. Mol. Microbiol. Biotechnol.'' '''3''':385-93</span>
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'''Seok, YJ, Koo, BM, Sondej, M and Peterkofsky, A'''  (2001) Regulation of E. coli glycogen phosphorylase activity by HPr. ''J. Mol. Microbiol. Biotechnol.'' '''3''':385-93
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!align=left  |Abstract
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Bacteria sense continuous changes in their environment and adapt metabolically to effectively compete with other organisms for limiting nutrients. One system which plays an important part in this adaptation response is the phosphoenol-pyruvate:sugar phosphotransferase system (PTS). Many proteins interact with and are regulated by PTS components in bacteria. Here we review the interaction with and allosteric regulation of Escherichia coli glycogen phosphorylase (GP) activity by the histidine phosphocarrier protein HPr, which acts as part of a phosphoryl shuttle between enzyme I and sugar-specific proteins of the PTS. HPr mediates crosstalk between PTS sugar uptake and glycogen breakdown. The evolution of the allosteric regulation of E. coli GP by HPr is compared to that of other phosphorylases.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11361069 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || Bacteria sense continuous changes in their environment and adapt metabolically to effectively compete with other organisms for limiting nutrients. One system which plays an important part in this adaptation response is the phosphoenol-pyruvate:sugar phosphotransferase system (PTS). Many proteins interact with and are regulated by PTS components in bacteria. Here we review the interaction with and allosteric regulation of Escherichia coli glycogen phosphorylase (GP) activity by the histidine phosphocarrier protein HPr, which acts as part of a phosphoryl shuttle between enzyme I and sugar-specific proteins of the PTS. HPr mediates crosstalk between PTS sugar uptake and glycogen breakdown. The evolution of the allosteric regulation of E. coli GP by HPr is compared to that of other phosphorylases.
!align=left  |Keywords
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Amino Acid Sequence; Bacterial Proteins; Conserved Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; Evolution, Molecular; Gene Expression Regulation, Bacterial; Molecular Sequence Data; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Phosphorylases/chemistry; Phosphorylases/genetics; Phosphorylases/metabolism; Sequence Alignment; Sequence Homology, Amino Acid
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11361069 PubMed]
 
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Latest revision as of 04:15, 15 September 2013

Citation

Seok, YJ, Koo, BM, Sondej, M and Peterkofsky, A (2001) Regulation of E. coli glycogen phosphorylase activity by HPr. J. Mol. Microbiol. Biotechnol. 3:385-93

Abstract

Bacteria sense continuous changes in their environment and adapt metabolically to effectively compete with other organisms for limiting nutrients. One system which plays an important part in this adaptation response is the phosphoenol-pyruvate:sugar phosphotransferase system (PTS). Many proteins interact with and are regulated by PTS components in bacteria. Here we review the interaction with and allosteric regulation of Escherichia coli glycogen phosphorylase (GP) activity by the histidine phosphocarrier protein HPr, which acts as part of a phosphoryl shuttle between enzyme I and sugar-specific proteins of the PTS. HPr mediates crosstalk between PTS sugar uptake and glycogen breakdown. The evolution of the allosteric regulation of E. coli GP by HPr is compared to that of other phosphorylases.

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Keywords

Amino Acid Sequence; Bacterial Proteins; Conserved Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; Evolution, Molecular; Gene Expression Regulation, Bacterial; Molecular Sequence Data; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Phosphorylases/chemistry; Phosphorylases/genetics; Phosphorylases/metabolism; Sequence Alignment; Sequence Homology, Amino Acid

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