Organic acid concentration is little controlled by phosphoenolpyruvate carboxylase activity in peach fruit

1999 ◽  
Vol 26 (6) ◽  
pp. 579 ◽  
Author(s):  
L. Svanella ◽  
M. Gaudillère ◽  
J. P. Gaudillère ◽  
A. Moing ◽  
R. Monet
Keyword(s):  
Organic Acid ◽  
Acid Concentration ◽  
Phosphoenolpyruvate Carboxylase ◽  
Prunus Persica ◽  
Carboxylase Activity ◽  
Acid Accumulation ◽  
Citrate Accumulation ◽  
Accumulation Phase

Changes in phosphoenolpyruvate carboxylase (PEPC) activity were studied during the fruit development of two peach cultivars (Prunus persica (L.) Batsch) with normal (‘Fantasia’) and low (‘Jalousia’) organic acid concentration. PEPC activities were measured in fruit mesocarp at two stages of development, corresponding to malate accumulation and citrate accumulation phases in ‘Fantasia’, respectively. In vitro activity, measured under optimal conditions, was significantly higher in ‘Fantasia’ than in ‘Jalousia’ during the malate accumulation phase but lower during the citrate accumulation phase. In vivo activity was estimated using 14CO2 labelling. The total incorporated radioactivity was higher in ‘Fantasia’ than in ‘Jalousia’ during the malate accumulation phase but lower during the citrate accumulation phase. During the malate accumulation phase, the partitioning of incorporated 14C into malate was significantly reduced in ‘Jalousia’ compared to ‘Fantasia’ after 20 min labelling. During the citrate accumulation phase, 14 C partitioning into malate was not significantly different between varieties, but partitioning into citrate was significantly reduced in ‘Jalousia’ compared to ‘Fantasia’. Therefore, PEPC activity does not seem to be the controlling step for the absence of organic acid accumulation in ‘Jalousia’ fruit. The other metabolic causes of the difference in organic acid accumulation are discussed; these may be connected with vacuolar storage.

scholarly journals Crude Citric Acid of Trichoderma asperellum: Tomato Growth Promotor and Suppressor of Fusarium oxysporum f. sp. lycopersici

Plants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 222
Author(s):  
Abdulaziz A. Al-Askar ◽  
WesamEldin I. A. Saber ◽  
Khalid M. Ghoneem ◽  
Elsayed E. Hafez ◽  
Amira A. Ibrahim
Keyword(s):  
Citric Acid ◽  
Plant Growth ◽  
Organic Acid ◽  
Wilt Disease ◽  
Growth And Yield ◽  
Total Phenolic ◽  
Growth Promoters ◽  
Chlorophyll Pigments

Presently, the bioprocessing of agricultural residues to various bioactive compounds is of great concern, with the potential to be used as plant growth promoters and as a reductive of various diseases. Lycopersiconesculentum, one of the most consumed crops in the human diet, is attacked by Fusarium wilt disease, so the main aim is to biocontrol the pathogen. Several fungal species were isolated from decayed maize stover (MS). Trichodermaasperellum was chosen based on its organic acid productivity and was molecularly identified (GenBank accession number is MW195019). Citric acid (CA) was the major detected organic acid by HPLC. In vitro, CA of T.asperellum at 75% completely repressed the growth of Fusariumoxysporum f. sp. lycopersici (FOL). In vivo, soaking tomato seeds in CA enhanced the seed germination and vigor index. T. asperellum and/or its CA suppressed the wilt disease caused by FOL compared to control. There was a proportional increment of plant growth and yield, as well as improvements in the biochemical parameters (chlorophyll pigments, total phenolic contents and peroxidase, and polyphenol oxidase activities), suggesting targeting both the bioconversion of MS into CA and biological control of FOL.

Phosphoenolpyruvate carboxylase during grape berry development: protein level, enzyme activity and regulation

2000 ◽  
Vol 27 (3) ◽  
pp. 221 ◽  
Author(s):  
Paraskevi Diakou ◽  
Laurence Svanella ◽  
Philippe Raymond ◽  
Jean-Pierre Gaudillère ◽  
Annick Moing
Keyword(s):  
Malic Acid ◽  
Protein Level ◽  
Phosphoenolpyruvate Carboxylase ◽  
Phosphorylation Site ◽  
Acid Synthesis ◽  
Grape Berry ◽  
Vitis Vinifera L ◽  
Normal Acid

The protein level and regulation of phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31, involved in malic acid synthesis) was studied during the fruit development of two grape (Vitis vinifera L.) varieties, ‘Cabernet Sauvignon’ and ‘Gora Chirine’, with berries of normal and low organic acid content, respectively. The protein level and in vitro activity were higher in the low-acid variety than in the normal-acid variety for most stages. In vivo PEPC activity, measured using 14 CO2 labelling, was significantly higher in the low-acid variety than in the normal-acid variety about 1 week before and 1 week after veraison (the day which corresponds to the onset of ripening). However, partitioning into malate was the same for both varieties. Antibodies raised against the N-terminal part of SorghumPEPC recognised the grape berry PEPC, indicating the presence of the consensus phosphorylation site involved in PEPC regulation. PEPC phosphorylation status was estimated by studying sensitivity to pH and malate. Grape berry PEPC appeared more sensitive to low pH and malate during ripening (IC50 malate, 0.2–0.7 mM) compared to during the earlier stages of development (IC50 malate, 1.2–2 mM) for both varieties. Therefore, in the normal-acid variety, PEPC seems to participate in controlling malic acid accumulation but does not seem to control the differences in malic acid concentration observed between the two varieties.

Polyamine metabolism during cardiac hypertrophy

1980 ◽  
Vol 239 (5) ◽  
pp. E372-E378 ◽  
Author(s):  
A. E. Pegg ◽  
H. Hibasami
Keyword(s):  
Cardiac Hypertrophy ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Elevated Concentration ◽  
Enzyme Protein ◽  
Carboxylase Activity ◽  
Rapid Reduction ◽  
Spermine Synthase

Treatment with thyroxine for 7 days to produce myocardial hypertrophy led to an increase in the content of putrescine, spermidine, and spermine in the rat heart. The content of decarboxylated S-adenosylmethionine, the source of the aminopropyl groups needed for polyamine synthesis, was increased by the thyroxine treatment as were the activities of ornithine and S-adenosylmethionine decarboxylases. The enhanced S-adenosylmethionine decarboxylase activity measured in vitro was due to an increase in the amount of enzyme protein as measured by immunotitration with a specific antiserum. In vivo, decarboxylation of S-adenosylmethionine was, therefore, increased both by the increased amount of enzyme protein and by the elevated concentration of putrescine (which activates the enzyme) brought about by the enhanced ornithine carboxylase activity. Spermine synthase did not change significantly during the treatment and spermidine synthase increased only slightly. Therefore, the accumulation of polyamines was mediated predominantly via the increased availability of both putrescine and decarboxylated S-adenosylmethionine. Administration of 1,3-diamino-2-propanol led to a rapid reduction in the activity of ornithine decarboxylase in the heart, and continued exposure to this substance by its inclusion in the drinking water completely prevented the increase in concentration of putrescine and polyamines in response to thyroxine. However, cardiac hypertrophy as measured by the increase in cardiac mass was not prevented by such treatment with 1,3-diaminopropanol, showing that the increased content of polyamines was not essential for the hypertrophic response.

scholarly journals Relationship between NH+4 Assimilation Rate and in Vivo Phosphoenolpyruvate Carboxylase Activity

1990 ◽  
Vol 94 (1) ◽  
pp. 284-290 ◽  
Author(s):  
Greg C. Vanlerberghe ◽  
Kathryn A. Schuller ◽  
Ronald G. Smith ◽  
Regina Feil ◽  
William C. Plaxton ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Assimilation Rate ◽  
Carboxylase Activity

EFFECTS OF OESTRADIOL ON WATER UPTAKE AND α-AMINOISOBUTYRIC ACID ACCUMULATION BY UTERI OF HEPATECTOMIZED RATS

1963 ◽  
Vol 28 (1) ◽  
pp. 73-78 ◽  
Author(s):  
J. R. DANIELS ◽  
S. M. KALMAN
Keyword(s):  
Inferior Vena ◽  
Vena Cava ◽  
Early Response ◽  
Isobutyric Acid ◽  
Acid Accumulation ◽  
One Step ◽  
Long Evans ◽  
Amino Isobutyric Acid

SUMMARY Adult Long Evans rats were ovariectomized and, one month later, were subjected to partial hepatectomy. Immature Long Evans rats were either partially hepatectomized in one step, or complete hepatectomy was accomplished by a two-stage operation which included ligation of the inferior vena cava followed by a partial evisceration. The response of these animals to injected oestradiol was compared with that of sham-operated controls by observing uptake of water by the uterus in vivo, and also by estimating the ability of surviving uterine fragments to accumulate radioactive α-amino-isobutyric acid in vitro. It was found that partial or complete hepatectomy did not abolish the response of the uterus to oestradiol. These results seem to exclude an essential role for the liver in the early response of a target organ to an oestrogenic hormone.

Intercellular Invertase in Developing Peach Mesocarp

1988 ◽  
Vol 15 (3) ◽  
pp. 377 ◽  
Author(s):  
TD Ugalde ◽  
DJ Chalmers ◽  
PH Jerie
Keyword(s):  
Dry Matter ◽  
Prunus Persica ◽  
Total Activity ◽  
Insoluble Fraction ◽  
Acid Invertase ◽  
Dry Matter Accumulation ◽  
Tissue Slices ◽  
Insoluble Particles

Acid invertase (β-fructofuranosidase, EC 3.2.1.26) was extracted from peach mesocarp (Prunus persica (L.) Batsch) using a range of extraction conditions. The enzyme always was attached to insoluble particles in the crude homogenate and was bound by a mechanism that could not have arisen during extraction. The activity in the insoluble fraction made up (essentially) all of the total activity extracted from the tissue and was the same as the activity shown by whole tissue slices placed directly into the assay solution. These results demonstrate that most of the acid invertase in developing peach mesocarp is located outside the cell. The amount of this enzyme, as measured in vitro, did not change during development at times when the rate of dry matter increase was changing rapidly. Either the action of intercellular invertase is not associated with the control of dry matter accumulation in peach mesocarp, or control is effected through activity of the enzyme in vivo, not its synthesis or degradation.

scholarly journals Presence of Acetyl Coenzyme A (CoA) Carboxylase and Propionyl-CoA Carboxylase in Autotrophic Crenarchaeota and Indication for Operation of a 3-Hydroxypropionate Cycle in Autotrophic Carbon Fixation

1999 ◽  
Vol 181 (4) ◽  
pp. 1088-1098 ◽  
Author(s):  
Castor Menendez ◽  
Zsuzsa Bauer ◽  
Harald Huber ◽  
Nasser Gad’on ◽  
Karl-Otto Stetter ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Carbon Fixation ◽  
Coenzyme A ◽  
Autotrophic Growth ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACT The pathway of autotrophic CO2 fixation was studied in the phototrophic bacterium Chloroflexus aurantiacus and in the aerobic thermoacidophilic archaeon Metallosphaera sedula. In both organisms, none of the key enzymes of the reductive pentose phosphate cycle, the reductive citric acid cycle, and the reductive acetyl coenzyme A (acetyl-CoA) pathway were detectable. However, cells contained the biotin-dependent acetyl-CoA carboxylase and propionyl-CoA carboxylase as well as phosphoenolpyruvate carboxylase. The specific enzyme activities of the carboxylases were high enough to explain the autotrophic growth rate via the 3-hydroxypropionate cycle. Extracts catalyzed the CO2-, MgATP-, and NADPH-dependent conversion of acetyl-CoA to 3-hydroxypropionate via malonyl-CoA and the conversion of this intermediate to succinate via propionyl-CoA. The labelled intermediates were detected in vitro with either 14CO2 or [14C]acetyl-CoA as precursor. These reactions are part of the 3-hydroxypropionate cycle, the autotrophic pathway proposed forC. aurantiacus. The investigation was extended to the autotrophic archaea Sulfolobus metallicus andAcidianus infernus, which showed acetyl-CoA and propionyl-CoA carboxylase activities in extracts of autotrophically grown cells. Acetyl-CoA carboxylase activity is unexpected in archaea since they do not contain fatty acids in their membranes. These aerobic archaea, as well as C. aurantiacus, were screened for biotin-containing proteins by the avidin-peroxidase test. They contained large amounts of a small biotin-carrying protein, which is most likely part of the acetyl-CoA and propionyl-CoA carboxylases. Other archaea reported to use one of the other known autotrophic pathways lacked such small biotin-containing proteins. These findings suggest that the aerobic autotrophic archaea M. sedula,S. metallicus, and A. infernus use a yet-to-be-defined 3-hydroxypropionate cycle for their autotrophic growth. Acetyl-CoA carboxylase and propionyl-CoA carboxylase are proposed to be the main CO2 fixation enzymes, and phosphoenolpyruvate carboxylase may have an anaplerotic function. The results also provide further support for the occurrence of the 3-hydroxypropionate cycle in C. aurantiacus.

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