Photosynthetic Enzyme Activities in the C3-C4 Intermediate Neurachne minor S. T . Blake (Poaceae)

1986 ◽  
Vol 13 (3) ◽  
pp. 399 ◽  
Author(s):  
PW Hattersley ◽  
NE Stone
Keyword(s):  
Malic Enzyme ◽  
Acid Decarboxylase ◽  
Decarboxylase Activity ◽  
Carboxylase Activity ◽  
Pep Carboxylase ◽  
C3 Plant ◽  
Bisphosphate Carboxylase ◽  
C3 Species ◽  
Species Activity ◽  
Pep Carboxykinase

The activities of eight key photosynthetic enzymes were measured in leaf blade extracts of the C3-C4 intermediate Neurachne minor S. T. Blake, its C3 and C4 relatives, C3-C4 Panicum milioides Nees ex Trin., and controls (all Poaceae). Phosphoenolpyruvate (PEP) carboxylase (PEPC) activity in N. minor (5.46 �mol mg Chl-1 min-1) is higher than previously reported for any other C3-C3 plant, and the ratio of ribulose-1,5-bisphosphate carboxylase activity to PEPC activity is lower than for P. milioides or C3 species. Activity of pyruvate,PI dikinase (up to 0.88 �mol mg Chl-1 min-1) is 3-5 times higher than in P. milioides. Assays of NADP-malic enzyme (NADP-ME), NAD-malic enzyme (NAD-ME) and PEP carboxykinase (PCK) show Paraneurachne muelleri (Hack.) S. T. Blake and Neurachne munroi (F. Muell.) F. Muell., N. minor's two close C4 relatives, to be NADP-ME type, as predicted from leaf anatomy. Aspartate and alanine aminotransferase activities in these species are higher than expected, however. N. minor (C3-C4) exhibits higher C4 acid decarboxylase activity than C3 species or P. milioides, for NADP-ME only (up to 1.07 �mol mg Chl-1 min-1). Our results suggest that N. minor possesses a limited C4 acid cycle, and that it is the most C4-like C3-C4 intermediate grass currently identified, comparable with some of the known C3-C4 Flaveria (Asteraceae) species.

Effect of Water Stress on Enzyme Activities in Wheat and Related Wild Species: Carboxylase Activity, Electron Transport and Photophosphorylation in Isolated Chloroplasts

1981 ◽  
Vol 8 (5) ◽  
pp. 385 ◽  
Author(s):  
ML Mayoral ◽  
D Atsmon ◽  
D Shimshi ◽  
Z Gromet-Elhanan
Keyword(s):  
Water Stress ◽  
Electron Transport ◽  
Clear Correlation ◽  
Initial Increase ◽  
Carboxylase Activity ◽  
Pep Carboxylase ◽  
Bisphosphate Carboxylase ◽  
Drought Sensitivity ◽  
Carboxylating Enzymes ◽  
Isolated Chloroplasts

Drought sensitivity of Triticum aestivum (cv. Sion) and two wild related species, T. longissimum and T. kotschyi was assessed by measuring the activity of ribulose-1,5-bisphosphate carboxylase (RuP2 carboxylase) and phosphoenolpyruvate carboxylase (PEP carboxylase), determination of total leaf soluble protein and chlorophyll content and by measuring the rates of electron transport and photophosphorylation in isolated chloroplasts. T. aestivum and T. longissimum showed relatively high drought sensitivity. The activity of the two carboxylating enzymes as well as chlorophyll and protein contents decreased with decreasing leaf water potential (Ψ). Rates of electron transport and photophosphorylation in isolated chloroplasts declined as soon as the Ψ value was reduced from - 0.8 MPa to - 1.0 MPa. In T. kotschyi, all the above activities remained stable down to a � value of about - 2 MPa. These results point to a clear correlation between the ability of T. kotschyi to grow in arid areas and its better performance in all the tests carried out under controlled water stress. In T. kotschyi an initial increase in PEP carboxylase activity was detected between Ψ values of -0.8 MPa and -2.1 MPa, followed by a sharp decline. No uncoupling of the chloroplasts by water stress was observed in any of the three species.

Role of salicylic acid in regulation of cadmium toxicity in wheat ( Triticum aestivum L.)

2009 ◽  
Vol 57 (3) ◽  
pp. 321-333 ◽  
Author(s):  
H. Moussa ◽  
S. EL-Gamal
Keyword(s):  
Pyruvate Carboxylase ◽  
Cadmium Toxicity ◽  
Triticum Aestivum L ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Cd Accumulation ◽  
Phosphoenol Pyruvate ◽  
Relative Water ◽  
Aba Content

Treatment with CdCl 2 (0, 100, 400 and 1000 μM) resulted in the inhibition of root dry biomass and root elongation and to increased Cd accumulation in the roots. These treatments also decreased the relative water content, chlorophyll content, 14 CO fixation, phosphoenol pyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase activity and abscisic acid (ABA) content, while increasing the malondialdehyde, hydrogen peroxide and free proline contents and causing changes in the chloroplast and root ultrastructure. Pretreatment of seeds with SA (500 μM) for 20 h resulted in the amelioration of these effects.

scholarly journals Ribulose 1,5-bisphosphate carboxylase. Effect on the catalytic properties of changing methionine-330 to leucine in the Rhodospirillum rubrum enzyme

1986 ◽  
Vol 235 (3) ◽  
pp. 839-846 ◽  
Author(s):  
B E Terzaghi ◽  
W A Laing ◽  
J T Christeller ◽  
G B Petersen ◽  
D F Hill
Keyword(s):  
Rhodospirillum Rubrum ◽  
Oligonucleotide Primer ◽  
Similar Amount ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate Carboxylase Oxygenase ◽  
In The Wild ◽  
The Stability

Oligonucleotide-directed mutagenesis of cloned Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase with a synthetic 13mer oligonucleotide primer was used to effect a change at Met-330 to Leu-330. The resultant enzyme was kinetically examined in some detail and the following changes were found. The Km(CO2) increased from 0.16 to 2.35 mM, the Km(ribulose bisphosphate) increased from 0.05 to 1.40 mM for the carboxylase reaction and by a similar amount for the oxygenase reaction. The Ki(O2) increased from 0.17 to 6.00 mM, but the ratio of carboxylase activity to oxygenase activity was scarcely affected by the change in amino acid. The binding of the transition state analogue 2-carboxyribitol 1,5-bisphosphate was reversible in the mutant and essentially irreversible in the wild type enzyme. Inhibition by fructose bisphosphate, competitive with ribulose bisphosphate, was slightly increased in the mutant enzyme. These data suggest that the change of the residue from methionine to leucine decreases the stability of the enediol reaction intermediate.

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