scholarly journals Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation.

1996 ◽  
Vol 178 (10) ◽  
pp. 2883-2889 ◽  
Author(s):  
M Birney ◽  
H D Um ◽  
C Klein
1967 ◽  
Vol 242 (15) ◽  
pp. 3531-3537
Author(s):  
John A. Grunau ◽  
Ernest Knight ◽  
Emily S. Hart ◽  
I.C. Gunsalus

1974 ◽  
Vol 52 (7) ◽  
pp. 594-598 ◽  
Author(s):  
Anita Krebs ◽  
William A. Bridger

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.


1967 ◽  
Vol 242 (10) ◽  
pp. 2474-2477
Author(s):  
Jane Gibson ◽  
Christen D. Upper ◽  
I.C. Gunsalus

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