| EC |
2.7.1.198 |
| Accepted name: |
protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase |
| Reaction: |
[protein]-Nπ-phospho-L-histidine + D-sorbitol[side 1] = [protein]-L-histidine + D-sorbitol 6-phosphate[side 2] |
| Other name(s): |
srlABE (gene names); D-sorbitol PTS permease; sorbitol PTS permease; glucitol PTS permease; EIIGut; Enzyme IIGut |
| Systematic name: |
protein-Nπ-phospho-L-histidine:D-sorbitol Nπ-phosphotransferase |
| Comments: |
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Lengeler, J. Nature and properties of hexitol transport systems in Escherichia coli. J. Bacteriol. 124 (1975) 39–47. [PMID: 1100608] |
| 2. |
Reizer, J., Mitchell, W.J., Minton, N., Brehm, J., Reizer, A. and Saier, M.H., Jr. Proposed topology of the glucitol permeases of Escherichia coli and Clostridium acetobutylicum. Curr. Microbiol. 33 (1996) 331–333. [PMID: 8875915] |
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| [EC 2.7.1.198 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.198] |
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