sugar phosphorylation
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2020 ◽  
Vol 11 ◽  
Author(s):  
Stefanie Wijnants ◽  
Michael Riedelberger ◽  
Philipp Penninger ◽  
Karl Kuchler ◽  
Patrick Van Dijck


2015 ◽  
Vol 25 (2-3) ◽  
pp. 73-78 ◽  
Author(s):  
Milton H. Saier Jr.

In 1964, Kundig, Ghosh and Roseman reported the discovery of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), which they subsequently proposed might catalyze sugar transport as well as sugar phosphorylation. What we have learned in the 50 years since its discovery is that, in addition to these primary functions, the PTS serves as a complex protein kinase system that regulates a wide variety of transport, metabolic and mutagenic processes as well as the expression of numerous genes. Recent operon- and genome-sequencing projects have revealed novel PTS protein-encoding genes, many of which have yet to be functionally defined. The current picture of the PTS is that of a complex system with ramifications in all aspects of cellular physiology. Moreover, its mosaic evolutionary history is unusual and intriguing. The PTS can be considered to serve many prokaryotes in capacities of communication and coordination, as do the nervous systems of animals.



2012 ◽  
Vol 47 (6) ◽  
pp. 843-846 ◽  
Author(s):  
W. Jiang ◽  
R. S. Pinder ◽  
J. A. Patterson ◽  
S. C. Ricke


2005 ◽  
Vol 187 (3) ◽  
pp. 890-901 ◽  
Author(s):  
Christopher J. Brigham ◽  
Michael H. Malamy

ABSTRACT Bacteroides fragilis, a human gastrointestinal commensal and an opportunistic pathogen, utilizes simple and complex sugars and polysaccharides for growth in the large intestine and at sites of infection. Because B. fragilis lacks transport-linked sugar phosphorylation systems, cytoplasmic kinase(s) was expected to be required for the phosphorylation of hexoses and hexosamines. We have now identified two hexose kinases that are important for growth of B. fragilis on glucose, mannose, and other sugars. One kinase (RokA), a member of the ROK family of proteins, was found to be the sole kinase for activation of N-acetyl-d-glucosamine (NAG). The other kinase (HexA) is responsible for the majority of the glucose kinase activity in the cell, although a hexA deletion mutant strain was not defective for growth on any substrate tested. Deletion of both the rokA and hexA kinase genes resulted in inability of the cell to use glucose, mannose, NAG, and many other sugars. We purified RokA and determined its approximate molecular mass to be 36.5 kDa. The purified RokA protein was shown to phosphorylate several substrates, including glucose, NAG, and mannose, but not N-acetylmannosamine or N-acetylneuraminic acid. Phylogenetic analysis of RokA showed that it is most similar to kinases from the Cytophaga-Flavibacterium-Bacteroides group, while HexA was most similar to other bacterial hexokinases and eukaryotic hexokinases.



1999 ◽  
Vol 105 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Antonio Galina ◽  
Carlos Logullo ◽  
Edmilson Fernandes de Souza ◽  
Gustavo Lazzaro Rezende ◽  
Wagner Seixas da Silva


Microbiology ◽  
1996 ◽  
Vol 142 (7) ◽  
pp. 1775-1782 ◽  
Author(s):  
M. B. Pernambuco ◽  
J. Winderickx ◽  
M. Crauwels ◽  
G. Griffioen ◽  
W. H. Mager ◽  
...  


Yeast ◽  
1994 ◽  
Vol 10 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Julián Nevado ◽  
MA Asunción Navarro ◽  
Claudio F. Heredia


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