PEP (phosphoenol pyruvate) group translocation, also known as the phosphotransferase system or PTS, is a distinct method used by bacteria for sugar uptake where the source of energy is from phosphoenolpyruvate (PEP). It is known to be a multicomponent system that always involves enzymes of the plasma membrane and those in the cytoplasm.
The PTS system uses active transport. After the translocation across the membrane, the metabolites transported are modified. The PTS system was discovered by Saul Roseman in 1964.[1] The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) transports and phosphorylates its sugar substrates in a single energy-coupled step. This transport process is dependent on several cytoplasmic phosphoryl transfer proteins - Enzyme I (I), HPr, Enzyme IIA (IIA), and Enzyme IIB (IIB)) as well as the integral membrane sugar permease (IIC).The PTS Enzyme II complexes are derived from independently evolving 4 PTS Enzyme II complex superfamilies, that include the (1) Glucose (Glc), (2) Mannose (Man),[2][3] (3) Ascorbate-Galactitol (Asc-Gat)[4][5] and (4) Dihydroxyacetone (DHA) superfamilies.[6][7]
^Bramley HF, Kornberg HL (July 1987). "Sequence homologies between proteins of bacterial phosphoenolpyruvate-dependent sugar phosphotransferase systems: identification of possible phosphate-carrying histidine residues". Proceedings of the National Academy of Sciences of the United States of America. 84 (14): 4777–80. Bibcode:1987PNAS...84.4777B. doi:10.1073/pnas.84.14.4777. PMC 305188. PMID 3299373.
^Liu, Xueli; Zeng, Jianwei; Huang, Kai; Wang, Jiawei (2019-06-17). "Structure of the mannose transporter of the bacterial phosphotransferase system". Cell Research. 29 (8): 680–682. doi:10.1038/s41422-019-0194-z. ISSN 1748-7838. PMC 6796895. PMID 31209249.
^Huang, Kai; Zeng, Jianwei; Liu, Xueli; Jiang, Tianyu; Wang, Jiawei (2021-04-06). "Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin". Cell Discovery. 7 (1): 20. doi:10.1038/s41421-021-00253-6. ISSN 2056-5968. PMC 8021565. PMID 33820910.
^Luo P, Yu X, Wang W, Fan S, Li X, Wang J (March 2015). "Crystal structure of a phosphorylation-coupled vitamin C transporter". Nature Structural & Molecular Biology. 22 (3): 238–41. doi:10.1038/nsmb.2975. PMID 25686089. S2CID 9955621.
^Luo P, Dai S, Zeng J, Duan J, Shi H, Wang J (2018). "Inward-facing conformation of l-ascorbate transporter suggests an elevator mechanism". Cell Discovery. 4: 35. doi:10.1038/s41421-018-0037-y. PMC 6048161. PMID 30038796.
^Saier MH (2015). "The Bacterial Phosphotransferase System: New frontiers 50 years after its discovery". Journal of Molecular Microbiology and Biotechnology. 25 (2–3): 73–78. doi:10.1159/000381215. PMC 4512285. PMID 26159069.
^Bächler C, Schneider P, Bähler P, Lustig A, Erni B (2005). "Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR". The EMBO Journal. 24 (2): 283–293. doi:10.1038/sj.emboj.7600517. PMC 545809. PMID 15616579.
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