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Structure and homologies of carbohydrate : phosphotransferase system (PTS) proteins

Title data

Lengeler, Joseph W. ; Titgemeyer, F. ; Vogler, A. P. ; Wöhrl, Birgitta:
Structure and homologies of carbohydrate : phosphotransferase system (PTS) proteins.
In: Philosophical Transactions of the Royal Society B: Biological Sciences. Vol. 326 (1990) Issue 1236 . - pp. 489-504.
ISSN 0962-8436
DOI: https://doi.org/10.1098/rstb.1990.0027

Abstract in another language

The bacterial phosphotransferase system (PTS) is the major transport system for many carbohydrates that are phosphorylated concomitantly with the translocation step through the membrane (group translocation). It consists of two general proteins, enzyme I and histidine protein (HPr), and a series of more than 15 substrate-specific enzymes II (EII). The sequences of several of these derived from Gram-positive and Gram-negative bacteria were compared, which allowed the possible identification of the following functional domains: membrane-bound pore, substrate-binding site, linker domains, transphosphorylation domain and primary phosphorylation site. Several EIIs have been analysed in the meantime, also by topological tests, by sequential deletion of the corresponding structural genes, and by construction of intergenic hybrids between different domains of several EIIs. These data suggest evolutionary relationships between different EIIs; they also enable a general model to be constructed of EIIs as carbohydrate transport systems, phosphotransferases, chemoreceptors in chemotaxis and as part of a global regulatory network.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Faculties
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 21 May 2019 06:58
Last Modified: 22 May 2019 05:24
URI: https://eref.uni-bayreuth.de/id/eprint/49033