The Effect of Metals on Maize (Zea mays) Phosphoenolpyruvate Carboxylase Isoenzymes

1984 ◽  
pp. 473-476 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase

Kinetic properties of recombinant phosphomimic mutant of Zea mays phosphoenolpyruvate carboxylase (ZmPEPCS15D)

2020 ◽  
Vol 25 (1) ◽  
pp. 1-8
Author(s):  
Madhurima Das ◽  
Mansi ◽  
Monika Dalal ◽  
Viswanathan Chinnusamy
Keyword(s):  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase ◽  
Kinetic Properties

Towards efficient photosynthesis: overexpression of Zea mays phosphoenolpyruvate carboxylase in Arabidopsis thaliana

2016 ◽  
Vol 130 (1-3) ◽  
pp. 47-72 ◽  
Author(s):  
Deepika Kandoi ◽  
Sasmita Mohanty ◽  
Govindjee ◽  
Baishnab C. Tripathy
Keyword(s):  
Arabidopsis Thaliana ◽  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase

Regulation of Phosphoenolpyruvate Carboxylase in Zea mays by Protein Phosphorylation and Metabolites and Their Roles in Photosynthesis

1996 ◽  
Vol 23 (1) ◽  
pp. 25 ◽  
Author(s):  
Y Gao ◽  
KC Woo
Keyword(s):  
Zea Mays ◽  
Enzyme Activity ◽  
Protein Phosphorylation ◽  
Photosynthetic Rate ◽  
Phosphoenolpyruvate Carboxylase ◽  
Strong Inhibitor ◽  
Physiological Concentration ◽  
Crude Extracts ◽  
Maize Leaves

The effects of metabolites, protein phosphorylation and malate inhibition on phosphoenolpyruvate carboxylase (PEPC) activity were investigated at pH 7.0 in partially purified enzyme from maize leaves. Glycine, glucose 6-phosphate or alanine stimulated the activity two- to three-fold. Glycine and glucose 6-phosphate increased the affinity for PEP by factors of eight and four respectively. These metabolites changed the response of the enzyme activity to pH. Activity increased between pH 6.8 and 8.0 by 10-fold in the absence and 26% in the presence of these metabolites. In vitro phosphorylation of PEPC increased the activity two-fold in the absence but not in the presence of these metabolites. Malate was a strong inhibitor of PEPC, the KI value being 0.25-0.5 mM. Protein phosphorylation and the above metabolites increased the Ki value by factors of three and 12 respectively, but they synergistically increased the Ki 50-fold, thus providing maximal protection against malate inhibition. In the crude extracts from light- and dark-adapted leaves in the presence of a physiological concentration of malate (20 mM), PEPC activity comparable to the photosynthetic rate was obtained only from the light-adapted leaves in the presence of metabolites indicating that both light-induced protein phosphorylation and metabolic activators were essential for PEPC activation during photosynthesis. We propose that both these factors act synergistically to modulate PEPC during photosynthesis in maize.

A kinetic investigation of phosphoenolpyruvate carboxylase from Zea mays

Biochemistry ◽  
1992 ◽  
Vol 31 (28) ◽  
pp. 6421-6426 ◽  
Author(s):  
James W. Janc ◽  
Marion H. O'Leary ◽  
W. W. Cleland
Keyword(s):  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase ◽  
Kinetic Investigation

A fundamental thermostable cyanide-sensitive phosphoenolpyruvate acid carboxylase in photosynthetic and other organisms

1971 ◽  
Vol 49 (4) ◽  
pp. 631-643 ◽  
Author(s):  
David Pan ◽  
E. Roy Waygood
Keyword(s):  
Heat Treatment ◽  
Zea Mays ◽  
Acid Phosphatase ◽  
Plant Species ◽  
Phosphoenolpyruvate Carboxylase ◽  
Deae Cellulose ◽  
Bundle Sheath ◽  
Evolutionary Significance ◽  
Optimum Temperature ◽  
Optimum Ph

A thermostable 'phosphoenolpyruvate carboxylase' has been isolated from leaves of Zea mays different from phosphoenolpyruvate carboxylase (EC. 4.1.1.31) in that its optimum pH is 5.4, it does not liberate orthophosphate during the reaction, and it is inhibited by cyanide. The enzymic reaction has an optimum temperature of 70–75C and has been purified through steps including acidification to pH 4.6, heat treatment to 50C, and DEAE-cellulose and Sephadex G-200 column chromatography. Three fractions were active in the Sephadex eluate, but only fraction III was free from a thermostable acid phosphatase which catalyzes the liberation of orthophosphate from the substrate and the end product which is suggested to be a C4 phosphocarbonyl compound, although phosphohydroxypyruvate appears by either spontaneous or enzymic decarboxylation. The enzyme is assayed by the formation of a phenyl-hydrazone at 325 nm. The enzyme is localized and tightly bound in both the parenchyma bundle sheath and mesophyll chloroplasts, which are free from the thermostable acid phosphatase. Similar concentrations of the enzyme have been found in all plant species tested including C3 plants, ferns, bryophytes, algae, fungi, and even in calf liver. The enzyme must have considerable evolutionary significance.

Carbon dioxide, the substrate for phosphoenolpyruvate carboxylase from leaves of maize

1969 ◽  
Vol 47 (9) ◽  
pp. 1455-1458 ◽  
Author(s):  
E. R. Waygood ◽  
Regis Mache ◽  
C. K. Tan
Keyword(s):  
Carbon Dioxide ◽  
Zea Mays ◽  
Carbonic Anhydrase ◽  
Phosphoenolpyruvate Carboxylase ◽  
Spinacea Oleracea ◽  
Natural Photosynthesis

Using a spectrophotometric technique it has been shown that CO2 is the substrate for phosphoenolpyruvate carboxylase (EC 4.1.1.31) from leaves of Zea mays. The Km (CO2) is approximately 7.5 × 10−6 M, which is the order of the half saturation value for CO2 in natural photosynthesis. Studies indicate also that carbonic anhydrase is localized in chloroplasts, isolated by the 'laceration technique' from leaves of Spinacea oleracea, but is absent from leaves of Zea mays. It is speculated that carbonic anhydrase catalyses a 'trap' for the CO2 escaping into the environment via photorespiration.

scholarly journals Cloning, Expression, and Characterization of a Root-Form Phosphoenolpyruvate Carboxylase from Zea mays: Comparison with the C4-Form Enzyme

1998 ◽  
Vol 39 (8) ◽  
pp. 865-873 ◽  
Author(s):  
L.-Y. Dong ◽  
T. Masuda ◽  
T. Kawamura ◽  
S. Hata ◽  
K. Izui
Keyword(s):  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase
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