New Paradigm for Allosteric Regulation of Escherichia coli Aspartate Transcarbamoylase

Biochemistry ◽  
2013 ◽  
Vol 52 (45) ◽  
pp. 8036-8047 ◽  
Author(s):  
Gregory M. Cockrell ◽  
Yunan Zheng ◽  
Wenyue Guo ◽  
Alexis W. Peterson ◽  
Jennifer K. Truong ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Allosteric Regulation ◽  
Aspartate Transcarbamoylase ◽  
New Paradigm

scholarly journals The Protein Interactome of Glycolysis in Escherichia coli

Proteomes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 16
Author(s):  
Shomeek Chowdhury ◽  
Stephen Hepper ◽  
Mudassir K. Lodi ◽  
Milton H. Saier ◽  
Peter Uetz
Keyword(s):  
Escherichia Coli ◽  
Protein Interactions ◽  
Allosteric Regulation ◽  
Glycolytic Enzymes ◽  
Protein Protein Interactions ◽  
Post Translational Modification ◽  
Interacting Protein ◽  
E Coli ◽  
Protein Interactome ◽  
The Impact

Glycolysis is regulated by numerous mechanisms including allosteric regulation, post-translational modification or protein-protein interactions (PPI). While glycolytic enzymes have been found to interact with hundreds of proteins, the impact of only some of these PPIs on glycolysis is well understood. Here we investigate which of these interactions may affect glycolysis in E. coli and possibly across numerous other bacteria, based on the stoichiometry of interacting protein pairs (from proteomic studies) and their conservation across bacteria. We present a list of 339 protein-protein interactions involving glycolytic enzymes but predict that ~70% of glycolytic interactors are not present in adequate amounts to have a significant impact on glycolysis. Finally, we identify a conserved but uncharacterized subset of interactions that are likely to affect glycolysis and deserve further study.

Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase

Biochemistry ◽  
1992 ◽  
Vol 31 (11) ◽  
pp. 3026-3032 ◽  
Author(s):  
Colin J. Newton ◽  
Raymond C. Stevens ◽  
Evan R. Kantrowitz
Keyword(s):  
Escherichia Coli ◽  
Aspartate Transcarbamoylase ◽  
Conserved Residue

scholarly journals Ligand interactions at the active site of aspartate transcarbamoylase from Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (7) ◽  
pp. 1605-1611 ◽  
Author(s):  
Paul R. Dennis ◽  
M. Vijaya Krishna ◽  
Maria Di Gregorio ◽  
William W. C. Chan
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Transcarbamoylase ◽  
Ligand Interactions
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