Relative Contribution of Ribulose 1,5-Diphosphate Carboxylase and Phosphoenolpyruvate Carboxylase to CO2 Fixation Activity in Roots of Dark-grown or Light-grown Lens culinaris Seedlings

1975 ◽  
Vol 34 (4) ◽  
pp. 309-313 ◽  
Author(s):  
A. NATO ◽  
E. DELEENS
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Lens Culinaris ◽  
Co2 Fixation ◽  
Relative Contribution ◽  
Fixation Activity

scholarly journals Anapleurotic CO2 Fixation by Phosphoenolpyruvate Carboxylase in C3 Plants

1987 ◽  
Vol 84 (1) ◽  
pp. 58-60 ◽  
Author(s):  
Eva Melzer ◽  
Marion H. O'Leary
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Co2 Fixation ◽  
C3 Plants

Inhibition of CO2 fixation in group D streptococci

1969 ◽  
Vol 15 (1) ◽  
pp. 57-60 ◽  
Author(s):  
Victor F. Lachica ◽  
Paul A. Hartman
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Pyruvate Carboxylase ◽  
Co2 Fixation ◽  
Tricarboxylic Acid Cycle ◽  
Inhibitory Effect ◽  
Tricarboxylic Acid ◽  
Acetyl Coa ◽  
Acid Cycle ◽  
Tricarboxylic Acid Cycle Intermediates ◽  
Group D

The stimulatory effect of acetyl-CoA and the inhibitory effect by L-aspartate and some intermediates of the tricarboxylic acid cycle in the assimilation of CO2 by crude extracts of group D streptococci suggest that the pyruvate carboxylase of Streptococcus faecium and the phosphoenolpyruvate carboxylase of S. bovis are allosteric enzymes. This implies that these enzymes are sites for the control of the amount of aspartate and of the tricarboxylic acid cycle intermediates synthesized.

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