Effects of temperature on the activity of phosphoenolpyruvate carboxylase and on the control of CO2 fixation in Bryophyllum fedtschenkoi

Planta ◽  
1995 ◽  
Vol 196 (2) ◽  
Author(s):  
PamelaJ. Carter ◽  
MalcolmB. Wilkins ◽  
HughG. Nimmo ◽  
CharlesA. Fewson
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Co2 Fixation ◽  
Effects Of Temperature

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.

scholarly journals Molecular Cloning of Novel-Type Phosphoenolpyruvate Carboxylase Isoforms in Pitaya (Hylocereus undatus)

Plants ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1241
Author(s):  
Keiichi Nomura ◽  
Yuho Sakurai ◽  
Mayu Dozono
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Co2 Fixation ◽  
Acid Metabolism ◽  
Regulation Mechanism ◽  
Amino Acid Residues ◽  
Plant Type ◽  
Allosteric Inhibitors ◽  
Hylocereus Undatus ◽  
Cam Photosynthesis ◽  
Important Enzyme

Phosphoenolpyruvate carboxylase (PEPC) is an important enzyme involved in the initial CO2 fixation of crassulacean acid metabolism (CAM) photosynthesis. To understand the cultivation characteristics of a CAM plant pitaya, it is necessary to clarify the characteristics of PEPC in this species. Here, we cloned three PEPC cDNAs in pitaya, HuPPC1, HuPPC2, and HuPPC3, which encode 942, 934, and 966 amino acid residues, respectively. Phylogenetic analysis indicated that these PEPC belonged to plant-type PEPC (PTPC), although HuPPC1 and HuPPC2 have no Ser-phosphorylation motif in N-terminal region, which is a crucial regulation site in PTPC and contributes to CAM periodicity. HuPPC1 and HuPPC2 phylogenetically unique to the Cactaceae family, whereas HuPPC3 was included in a CAM clade. Two isoforms were partially purified at the protein level and were assigned as HuPPC2 and HuPPC3 using MASCOT analysis. The most distinct difference in enzymatic properties between the two was sensitivity to malate and aspartate, both of which are allosteric inhibitors of PEPC. With 2 mM malate, HuPPC3 was inhibited to 10% of the initial activity, whereas HuPPC2 activity was maintained at 70%. Aspartate inhibited HuPPC3 activity by approximately 50% at 5 mM; however, such inhibition was not observed for HuPPC2 at 10 mM. These results suggest that HuPPC3 corresponds to a general CAM-related PEPC, whereas HuPPC1 and HuPPC2 are related to carbon and/or nitrogen metabolism, with a characteristic regulation mechanism similar to those of Cactaceae plants.

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