Category:Complex:EIITre
About
Description (originally from EcoCyc[1]) EIITre
Description (originally from EcoCyc[2]) trehalose PTS permease
Comments (originally from EcoCyc[1][2]) TreB, the trehalose PTS permease, belongs to the functional superfamily of the phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The PTS transports and simultaneously phosphorylates its sugar substrates in a process called group translocation. TreB together with IIAGlc takes up exogenous trehalose, releasing the phosphate ester into the cell cytoplasm in preparation for hydrolysis via phosphotrehalase (TreA). Subsequent metabolism occurs primarily via glycolysis
[3][4][5] . The monocistronic treR
operon, encoding the repressor of the treBC operon is upstream of the treBC operon and is transcribed in the same direction. tre operon expression is under the control of the cyclic AMP-cyclic AMP receptor protein (CRP) complex as well as that of TreR. Metabolism of trehalose can occur either by a PTS-dependent (low trehalose concentrations) or a PTS-independent (high trehalose concentrations) mechanism. The latter process involves periplasmic hydrolysis of trehalose to glucose.
References
- ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Postma, PW et al. (1993) Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57 543-94 PubMed
- ↑ Klein, W et al. (1995) Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose. J. Bacteriol. 177 4043-52 PubMed
- ↑ Rimmele, M & Boos, W (1994) Trehalose-6-phosphate hydrolase of Escherichia coli. J. Bacteriol. 176 5654-64 PubMed
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