Escherichia coli coenzyme A-transferase: Kinetics, catalytic pathway and structure

1975 ◽  
Vol 171 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Stephen J. Sramek ◽  
Frank E. Frerman
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A

scholarly journals Succinyl Coenzyme A Synthetase from Escherichia coli

1967 ◽  
Vol 242 (15) ◽  
pp. 3531-3537
Author(s):  
John A. Grunau ◽  
Ernest Knight ◽  
Emily S. Hart ◽  
I.C. Gunsalus
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Succinyl Coenzyme A Synthetase

scholarly journals Mutants of Escherichia coli with Temperature-sensitive Malonyl Coenzyme A-Acyl Carrier Protein Transacylase

1974 ◽  
Vol 249 (23) ◽  
pp. 7468-7475
Author(s):  
Mark E. Harder ◽  
Ruth C. Ladenson ◽  
Steven D. Schimmel ◽  
David F. Silbert
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Temperature Sensitive ◽  
Carrier Protein

Genetic studies of the role of fatty acid and coenzyme A in photocatalytic inactivation of Escherichia coli

2012 ◽  
Vol 46 (13) ◽  
pp. 3951-3957 ◽  
Author(s):  
Minghui Gao ◽  
Taicheng An ◽  
Guiying Li ◽  
Xin Nie ◽  
Ho-Yin Yip ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Coenzyme A ◽  
Genetic Studies ◽  
Photocatalytic Inactivation

scholarly journals Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli

2019 ◽  
Vol 75 (6) ◽  
pp. 545-553 ◽  
Author(s):  
Ekaterina V. Filippova ◽  
Steven Weigand ◽  
Olga Kiryukhina ◽  
Alan J. Wolfe ◽  
Wayne F. Anderson
Keyword(s):  
Escherichia Coli ◽  
Vibrio Cholerae ◽  
Crystal Structures ◽  
Coenzyme A ◽  
Amino Group ◽  
Acetyl Coenzyme A ◽  
E Coli ◽  
Ligand Free ◽  
Acetyl Group ◽  
Terminal Amino

Spermidine N-acetyltransferase (SpeG) transfers an acetyl group from acetyl-coenzyme A to an N-terminal amino group of intracellular spermidine. This acetylation inactivates spermidine, reducing the polyamine toxicity that tends to occur under certain chemical and physical stresses. The structure of the SpeG protein from Vibrio cholerae has been characterized: while the monomer possesses a structural fold similar to those of other Gcn5-related N-acetyltransferase superfamily members, its dodecameric structure remains exceptional. In this paper, structural analyses of SpeG isolated from Escherichia coli are described. Like V. cholerae SpeG, E. coli SpeG forms dodecamers, as revealed by two crystal structures of the ligand-free E. coli SpeG dodecamer determined at 1.75 and 2.9 Å resolution. Although both V. cholerae SpeG and E. coli SpeG can adopt an asymmetric open dodecameric state, solution analysis showed that the oligomeric composition of ligand-free E. coli SpeG differs from that of ligand-free V. cholerae SpeG. Based on these data, it is proposed that the equilibrium balance of SpeG oligomers in the absence of ligands differs from one species to another and thus might be important for SpeG function.

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