scholarly journals Succinyl-Coenzyme A Synthetase and its Role in δ-Aminolevulinic Acid Biosynthesis in Euglena gracilis

1992 ◽  
Vol 99 (2) ◽  
pp. 482-487 ◽  
Author(s):  
Sandra M. Mayer ◽  
Samuel I. Beale
Keyword(s):  
Euglena Gracilis ◽  
Coenzyme A ◽  
Aminolevulinic Acid ◽  
Acid Biosynthesis ◽  
Succinyl Coenzyme A Synthetase

scholarly journals δ-Aminolevulinic Acid Biosynthesis from Glutamatein Euglena gracilis

1991 ◽  
Vol 97 (3) ◽  
pp. 1094-1102 ◽  
Author(s):  
Sandra M. Mayer ◽  
Samuel I. Beale
Keyword(s):  
Euglena Gracilis ◽  
Aminolevulinic Acid ◽  
Acid Biosynthesis

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 LCAA, a Novel Factor Required for Magnesium Protoporphyrin Monomethylester Cyclase Accumulation and Feedback Control of Aminolevulinic Acid Biosynthesis in Tobacco

2012 ◽  
Vol 160 (4) ◽  
pp. 1923-1939 ◽  
Author(s):  
Christin Anne Albus ◽  
Annabel Salinas ◽  
Olaf Czarnecki ◽  
Sabine Kahlau ◽  
Maxi Rothbart ◽  
...  
Keyword(s):  
Feedback Control ◽  
Aminolevulinic Acid ◽  
Acid Biosynthesis

Succinyl Coenzyme A Synthetase of Escherichia coli: Initial Rate Kinetics of Succinyl-CoA Cleavage and Isotope Exchange Studies

1973 ◽  
Vol 51 (1) ◽  
pp. 44-55 ◽  
Author(s):  
Frank J. Moffet ◽  
W. A. Bridger
Keyword(s):  
Isotope Exchange ◽  
Coenzyme A ◽  
Initial Rate ◽  
Substrate Inhibition ◽  
Kinetic Studies ◽  
Kinetic Mechanism ◽  
Constant Ratio ◽  
Rate Kinetics ◽  
Kinetics Of ◽  
Succinyl Coenzyme A Synthetase

Initial rate kinetic studies of succinyl coenzyme A synthetase of E. coli in the direction of succinyl-CoA cleavage are consistent with the operation of a partially random sequential kinetic mechanism with initial binding of ADP followed by random association of succinyl-CoA and Pi. The mechanism is analogous to that proposed previously for the succinyl-CoA formation reaction, and thus the kinetic mechanism of the overall reversible succinyl-CoA synthetase reaction appears to be symmetrical.Studies of the kinetics of [Formula: see text] isotope exchange at equilibrium show that this partially random sequential kinetic mechanism is not an exclusive pathway. [Formula: see text] isotope exchange rates did not show complete substrate inhibition when CoA or succinate was varied in constant ratio with Pi. However, when CoA or succinate was varied in constant ratio with succinyl-CoA, nearly complete substrate inhibition was observed. These results can be interpreted in terms of a wide variety of minor pathways of substrate binding and product release available to the enzyme under various conditions.

Sign in / Sign up

Export Citation Format

Share Document