Reaction: protein Nπ-phospho-L-histidine + sugar = protein histidine + sugar phosphate
Other name(s): glucose permease; PTS permease; phosphotransferase, phosphohistidinoprotein-hexose; enzyme IIl4ac; gene glC proteins; gene bglC RNA formation factors; PEP-dependent phosphotransferase enzyme II; PEP-sugar phosphotransferase enzyme II; phosphoenolpyruvate-sugar phosphotransferase enzyme II; phosphohistidinoprotein-hexose phosphotransferase; phosphohistidinoprotein-hexose phosphoribosyltransferase; phosphoprotein factor-hexose phosophotransferase; protein, specific or class, gene bglC; ribonucleic acid formation factor, gene glC; sucrose phosphotransferase system II; protein-Nπ-phosphohistidine:sugar N-pros-phosphotransferase; protein-Nπ-phosphohistidine:sugar Nπ-phosphotransferase
Systematic name: protein-Nπ-phospho-L-histidine:sugar Nπ-phosphotransferase
Comments: Enzyme II of the phosphotransferase system. Comprises a group of related enzymes. The protein substrate is a phosphocarrier protein of low molecular mass (9.5 kDa). The protein is phosphorylated in a reaction catalysed by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase) and this acts as the phosphate donor for the above reaction. The enzyme translocates the sugar it phosphorylates into bacteria. Aldohexoses, and their glycosides and alditols, are phosphorylated on O-6, whereas fructose and sorbose are phosphorylated on O-1. Glycerone and disaccharides are also substrates.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37278-09-4
References:
1. Kornberg, H.L. and Riordan, C. Uptake of galactose into Escherichia coli by facilitated diffusion. J. Gen. Microbiol. 94 (1976) 75-89. [PMID: 778334]
2. Postma, P.W. and Roseman, S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta 457 (1976) 213-257. [PMID: 187249]