scholarly journals Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter.

1997 ◽  
Vol 179 (13) ◽  
pp. 4138-4142 ◽  
Author(s):  
S J Park ◽  
G Chao ◽  
R P Gunsalus
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Alpha Ketoglutarate Dehydrogenase ◽  
Succinyl Coenzyme A Synthetase ◽  
Ketoglutarate Dehydrogenase

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

Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and .alpha.-ketoglutarate dehydrogenase complexes of Escherichia coli

Biochemistry ◽  
1981 ◽  
Vol 20 (16) ◽  
pp. 4555-4560 ◽  
Author(s):  
Larry R. Stepp ◽  
Dennis M. Bleile ◽  
Donald K. McRorie ◽  
Flora H. Pettit ◽  
Lester J. Reed
Keyword(s):  
Escherichia Coli ◽  
Lipoic Acid ◽  
Alpha Ketoglutarate Dehydrogenase ◽  
Ketoglutarate Dehydrogenase

Some Physical Parameters of Succinyl-Coenzyme A Synthetase of Escherichia coli

1974 ◽  
Vol 52 (7) ◽  
pp. 594-598 ◽  
Author(s):  
Anita Krebs ◽  
William A. Bridger
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Coenzyme A ◽  
Apparent Molecular Weight ◽  
Random Coil ◽  
Sedimentation Equilibrium ◽  
Physical Parameters ◽  
Equilibrium Studies ◽  
Α Helix ◽  
Succinyl Coenzyme A Synthetase

A physical study of succinyl-coenzyme A synthetase of Escherichia coli has been conducted. The extinction coefficient for the enzyme at 280 nm [Formula: see text] has been evaluated by two independent methods and found to be equal to 4.9 ± 0.2. Sedimentation equilibrium studies show that there is a marked dependence of the apparent molecular weight upon the concentration of the enzyme. At concentrations above 1 mg/ml, the enzyme exists predominantly as an α2β2 tetramer of overall molecular weight near 140 000; at lower concentrations, a significant fraction of the enzyme dissociates to an αβ dimer. The circular dichroism spectrum of the enzyme suggests a high proportion of random coil structure, with small contributions of α-helix and β-structure.

scholarly journals Succinyl Coenzyme A Synthetase from Escherichia coli

1967 ◽  
Vol 242 (10) ◽  
pp. 2474-2477
Author(s):  
Jane Gibson ◽  
Christen D. Upper ◽  
I.C. Gunsalus
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Succinyl Coenzyme A Synthetase
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