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malfunction
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disruption of glcG gene, encoding enzyme II of the D-glucose phosphoenolpyruvate-dependent phosphotransferase system (PTS), results in greatly improved D-xylose and L-arabinose consumption in the presence of D-glucose. Despite the loss of GlcG, the resulting mutant strain 824glcG ferments D-glucose as efficiently as the parent strain, overview
malfunction
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enhancement of Crp (crp+) in mgsA, pgi, and ptsG mutants, resulting in derivative strains that abolish CCR and induce exclusion mechanisms, allowing the simultaneous consumption of mixtures of sugars with low acetate production
metabolism
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correlation between the activity of the EIICBGlc and the phosphorylation level of the EIIAGlc
metabolism
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the enzyme is involved in the uptake and metabolism of D-glucose and other carbphydrates as part of the phosphoenolpyruvate-carbohydrate phosphotransferase system , PTS, detailed overview. Carbon catabolite repression,CCR, regulation is modulated by the phosphorylation state of EIIAGlc
physiological function
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in Escherichia coli, the phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS), including the enzyme activity of EC 2.7.1.69, is responsible for the transport and phosphorylation of sugars, such as glucose. PTS activity has a crucial role in the global signaling system that controls the preferential consumption of glucose over other carbon sources. When the cell is exposed to carbohydrate mixtures, the PTS prevents the expression of catabolic genes and activity of non-PTS sugars transport systems by carbon catabolite repression, CCR, mechanism, overview. EIIAGlc and EIIBGlc exhibit allosteric regulation on adenylate cyclase, and LacY, a specific transporter for lactose, overview. conditional binding of EIIAGlc to LacY in the presence of lactose avoids waste of this PTS component if the non-PTS substrate is not present in the environment. Regulatory functions of PTS, e.g. on Mlc, overview
physiological function
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In the phosphoenolpyruvate-dependent phosphotransferase system, PTS, system, Enzyme I catalyzes the transfer of the phosphate group from phosphoenolpyruvate to a nitrogen atom of a histidine moiety in a small protein (HPr). In subsequent processes , the appropriate Enzyme II catalyzes the transfer of phosphate from the phosphorylated protein (phospho-HPr) to its specific sugar acceptor, with D-glucose being preferred as substrate compared to sucrose. Regulation of a sucrose PTS in acid-forming clostridia, overview
physiological function
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the glycolytic intermediate glucose-6-phosphate is derived from EII-mediated phosphorylation during D-glucose uptake
physiological function
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the phosphoenolpyruvate-dependent-carbohydrate:phosphotransferase systems (PTSs) of enteric bacteria constitute a complex transport and sensory system. Such a PTS usually consists of two cytoplasmic energy-coupling proteins, Enzyme I (EI) and HPr, and one of more than 20 different carbohydrate-specific membrane proteins named Enzyme II (EII), which catalyze the uptake and concomitant phosphorylation of numerous carbohydrates. All phosphotransfer reactions between PEP and the EIIB domains of any carbohydrate-specific EII are reversible, only the final step, i.e., the transfer of the high-energy phosphate group to the substrate, is virtually irreversible. The glucose-PTS uses a PTS-typical phosphorylation cascade to transport and phosphorylate glucose, very complex regulation of the ptsG gene and the PTS system, detailed overview
physiological function
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In the phosphoenolpyruvate-dependent phosphotransferase system, PTS, system, Enzyme I catalyzes the transfer of the phosphate group from phosphoenolpyruvate to a nitrogen atom of a histidine moiety in a small protein (HPr). In subsequent processes , the appropriate Enzyme II catalyzes the transfer of phosphate from the phosphorylated protein (phospho-HPr) to its specific sugar acceptor, with D-glucose being preferred as substrate compared to sucrose. Regulation of a sucrose PTS in acid-forming clostridia, overview
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additional information
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during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript. Functional involvement of this putative PTS and of 1-PFK and FBA in fructose degradation, modeling, overview
additional information
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membrane-bound EIICGlc and EIIBGlc components conforming the EIICBGlc
additional information
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the enzyme belongs to the D-glucose phosphoenolpyruvate-dependent phosphotransferase system , PTS, typical PTS contains enzyme I (EI), enzyme II (EII, EC 2.7.1.69) and a histidine-containing protein (HPr)
additional information
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during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript. Functional involvement of this putative PTS and of 1-PFK and FBA in fructose degradation, modeling, overview
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during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript
in the absence of glucose, ptsG expression is repressed by Mlc
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in the presence of glucose, Mlc is sequestered by the dephosphorylated transporter EIICBGlc, which leads to an enhanced ptsG transcription
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ptsG expression is regulated in multiple ways, overview
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during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript
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during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript
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