Carbohydrate Transport by Group Translocation: The Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System
Abstract
The Bacterial Phosphoenolpyruvate (PEP) : Sugar Phosphotransferase System (PTS) mediates the uptake and phosphorylation of carbohydrates, and controls the carbon- and nitrogen metabolism in response to the availability of sugars. PTS occur in eubacteria and in a few archaebacteria but not in animals and plants. All PTS comprise two cytoplasmic phosphotransferase proteins (EI and HPr) and a species-dependent, variable number of sugar-specific enzyme II complexes (IIA, IIB, IIC, IID). EI and HPr transfer phosphorylgroups from PEP to the IIA units. Cytoplasmic IIA and IIB units sequentially transfer phosphates to the sugar, which is transported by the IIC and IICIID integral membrane protein complexes. Phosphorylation by IIB and translocation by IIC(IID) are tightly coupled. The IIC(IID) sugar transporters of the PTS are in the focus of this review. There are four structurally different PTS transporter superfamilies (glucose, glucitol, ascorbate, mannose) . Crystal structures are available for transporters of two superfamilies: bcIIC mal (MalT, 5IWS, 6BVG) and bcIIC chb (ChbC, 3QNQ) of B. subtilis from the glucose family, and IIC asc (UlaA, 4RP9, 5ZOV) of E. coli from the ascorbate superfamily . They are homodimers and each protomer has an independent transport pathway which functions by an elevator-type alternating-access mechanism. bcIIC mal and bcIIC chb have the same fold, IIC asc has a completely different fold. Biochemical and biophysical data accumulated in the past with…
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The genes for each phosphorelay enzyme present in JCVI-syn3A are considered essential in the genome-wide transposon mutagenesis essentiality study and structures are known for each component in other bacteria.
“The genes for each of the phosphorelay enzymes present in JCVI-syn3A are considered essential in the genome-wide transposon mutagenesis essentiality study and structures are known for each component in other bacteria (Breuer et al., 2019; Jeckelmann and Erni, 2019).”
From Fundamental behaviors emerge from simulations of a living minimal cell (2022) · cites this paper as Jeckelmann and Erni, 2019
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- Authors
- Jeckelmann, J.-M., & Erni, B.
- Affiliations
- University of Bern (CH)
- Corresponding author
- Jeckelmann, Jean-Marc
- Venue
- Subcellular Biochemistry
- Publisher
- Springer International Publishing
- Published
- 2019
- Volume
- 92
- Pages
- 223-274
- ISSN
- 0306-0225 (ISSN-L)
- OpenAlex
- W2952741822
- Cited by
- 55
- References
- 249
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 9 · 2023: 8 · 2022: 6 · 2021: 2 · 2020: 11 · 2019: 2
- FWCI
- 13.05
- Type
- book chapter
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Bern Open Repository and Information System (University of Bern) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- phosphoenolpyruvate-dependent phosphotransferase system, group translocation, carbohydrate transport, sugar phosphorylation, alternating access mechanism, Escherichia coli, Bacillus subtilis
- MeSH terms
- Sugars, Bacteria, Biological Transport, Phosphoenolpyruvate Sugar Phosphotransferase System, Phosphorylation
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