Degradation of -Glutamate Dehydrogenase from Escherichia coli: Allosteric Regulation of Enzyme Stability

2002 ◽  
Vol 397 (2) ◽  
pp. 206-216 ◽  
Author(s):  
Michael R. Maurizi ◽  
Fatima Rasulova
Keyword(s):  
Escherichia Coli ◽  
Glutamate Dehydrogenase ◽  
Enzyme Stability ◽  
Allosteric Regulation

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.

The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase

1993 ◽  
Vol 240 (2) ◽  
pp. 286-289 ◽  
Author(s):  
Kerrie M. Jones ◽  
Michael J. McPherson ◽  
Andrew J. Baron ◽  
Iain W. Mattaj ◽  
Claudia L. Riordan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Glutamate Dehydrogenase ◽  
Point Mutation ◽  
Lysine Residue ◽  
Escherichia Coli K12

scholarly journals The structure and allosteric regulation of mammalian glutamate dehydrogenase

2012 ◽  
Vol 519 (2) ◽  
pp. 69-80 ◽  
Author(s):  
Ming Li ◽  
Changhong Li ◽  
Aron Allen ◽  
Charles A. Stanley ◽  
Thomas J. Smith
Keyword(s):  
Glutamate Dehydrogenase ◽  
Allosteric Regulation

Expression of Psychrophilic Genes in Mesophilic Hosts: Assessment of the Folding State of a Recombinant α-Amylase

1998 ◽  
Vol 64 (3) ◽  
pp. 1163-1165 ◽  
Author(s):  
Georges Feller ◽  
Olivier Le Bussy ◽  
Charles Gerday
Keyword(s):  
Escherichia Coli ◽  
Enzyme Stability ◽  
Expression System ◽  
Wild Strain ◽  
Culture Temperature ◽  
E Coli ◽  
System A ◽  
Irreversible Denaturation ◽  
The Antarctic ◽  
Folding State

ABSTRACT α-Amylase from the antarctic psychrophile Alteromonas haloplanktis is synthesized at 0 ± 2°C by the wild strain. This heat-labile α-amylase folds correctly when overexpressed in Escherichia coli, providing the culture temperature is sufficiently low to avoid irreversible denaturation. In the described expression system, a compromise between enzyme stability and E. coli growth rate is reached at 18°C.

Reduction of Δ1-pyrroline-2-carboxylic acid to proline in escherichia coli: lack of involvement of glutamate dehydrogenase and Δ1-pyrroline-5-carboxylate reductase.

1993 ◽  
Vol 3 (6) ◽  
pp. 1197-1202 ◽  
Author(s):  
Mark L. Lewis ◽  
Steve L. Martin ◽  
Christine J. Rowe ◽  
John D. Sutherland ◽  
Esther J. Wilson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Carboxylic Acid ◽  
Glutamate Dehydrogenase ◽  
Carboxylate Reductase
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