scholarly journals Lack of fructose-1,6-bisphosphatase in a range of higher plants that store starch

1990 ◽  
Vol 271 (2) ◽  
pp. 467-472 ◽  
Author(s):  
G Entwistle ◽  
T ap Rees
Keyword(s):  
Potato Tuber ◽  
Sweet Corn ◽  
Higher Plants ◽  
Starch Synthesis ◽  
Significant Activity ◽  
Higher Plant ◽  
White Horse ◽  
Fructose 1,6 Bisphosphatase ◽  
Pea Roots ◽  
Fructose 1,6 Bisphosphate

The aim of this work was to discover whether fructose-1,6-bisphosphatase (FBPase) is present in higher-plant cells that synthesize storage starch. The following were examined: suspension cultures of soybean (Glycine max), tubers of potato (Solanum tuberosum), florets of cauliflower (Brassica oleracea), developing endosperm of maize and of sweet corn (Zea mays), roots of pea (Pisum sativum), and the developing embryos of round and wrinkled varieties of pea. Unfractionated extracts of each tissue readily converted fructose 1,6-bisphosphate to fructose 6-phosphate in assays for both plastidic and cytosolic FBPase. These conversions were not inhibited by 20 microM-fructose 2,6-bisphosphate. Except in extracts of pea embryos and sweet-corn endosperm, treatment with affinity-purified antibodies to pyrophosphate: fructose-6-phosphate 1-phosphotransferase reduced the above fructose 6-phosphate production to the rate found with boiled extracts. The antibody-resistant activity from sweet corn was slight. In immunoblot analyses, antibody to plastidic FBPase did not react positively with any protein in extracts of soybean cells, potato tuber, cauliflower florets, maize endosperm and pea roots. Positive reactions were found for extracts of embryos of both round and wrinkled varieties of peas and endosperm of sweet corn. For pea embryos, but not for sweet-corn endosperm, the Mr of the recognized protein corresponded to that of plastidic FBPase. It is argued that soybean cells, potato tuber, cauliflower florets, maize (var. White Horse Tooth) endosperm and pea roots lack significant activity of plastidic FBPase, but that this enzyme is present in developing embryos of pea. The data for sweet corn (var. Golden Bantam) are not decisive. It is also argued that, where FBPase is absent, carbon for starch synthesis does not enter the amyloplast as triose phosphate.

scholarly journals Pyrophosphate:fructose 6-phosphate 1-phosphotransferase and glycolysis in non-photosynthetic tissues of higher plants

1985 ◽  
Vol 227 (1) ◽  
pp. 299-304 ◽  
Author(s):  
T ap Rees ◽  
J H Green ◽  
P M Wilson
Keyword(s):  
Pisum Sativum ◽  
Beta Vulgaris ◽  
Higher Plants ◽  
Starch Synthesis ◽  
Carbohydrate Oxidation ◽  
Allium Porrum ◽  
Catalytic Activities ◽  
Net Flux ◽  
Arum Maculatum ◽  
Fructose 1,6 Bisphosphate

The activity of pyrophosphate:fructose-6-phosphate 1-phosphotransferase [PFK (PPi); EC 2.7.1.90] in extracts of the storage tissues of leek (Allium porrum), beetroot (Beta vulgaris) and roots of darnel (Lolium temulentum) exceeded 0.15 mumol/min per g fresh wt. As net flux from fructose 1,6-bisphosphate to fructose 6-phosphate in these tissues is unlikely, it is suggested that PFK (PPi) does not contribute to gluconeogenesis or starch synthesis. The maximum catalytic activities of PFK (PPi) in apex, stele and cortex of the root of pea (Pisum sativum) and in the developing and the thermogenic club of the spadix of cuckoo-pint (Arum maculatum) were measured and compared with those of phosphofructokinase, and to estimates of the rates of carbohydrate oxidation. PPi and fructose 2,6-bisphosphate in Arum clubs were measured. The above measurements are consistent with a glycolytic role for PFK (PPi) in tissues where there is marked biosynthesis, but not in the thermogenic club of Arum. The possibility that PFK (PPi) is a means of synthesizing pyrophosphate is discussed.

scholarly journals Sweet Corn Research around the World 2015–2020

Agronomy ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 534
Author(s):  
Pedro Revilla ◽  
Calli M. Anibas ◽  
William F. Tracy
Keyword(s):  
Sweet Corn ◽  
Starch Content ◽  
Starch Synthesis ◽  
Environmental Care ◽  
Research Activities ◽  
The Us ◽  
The World ◽  
The Usa ◽  
Basic Biology ◽  
Endosperm Starch

Modern sweet corn is distinguished from other vegetable corns by the presence of one or more recessive alleles within the maize endosperm starch synthesis pathway. This results in reduced starch content and increased sugar concentration when consumed fresh. Fresh sweet corn originated in the USA and has since been introduced in countries around the World with increasing popularity as a favored vegetable choice. Several reviews have been published recently on endosperm genetics, breeding, and physiology that focus on the basic biology and uses in the US. However, new questions concerning sustainability, environmental care, and climate change, along with the introduction of sweet corn in other countries have produced a variety of new uses and research activities. This review is a summary of the sweet corn research published during the five years preceding 2021.

Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.)

2002 ◽  
Vol 362 (2) ◽  
pp. 423-432 ◽  
Author(s):  
Johanna E. CORNAH ◽  
Jennifer M. ROPER ◽  
Davinder Pal SINGH ◽  
Alison G. SMITH
Keyword(s):  
Ferrous Iron ◽  
Specific Activity ◽  
Higher Plants ◽  
Protoporphyrin Ix ◽  
Chlorophyll Synthesis ◽  
Marker Enzyme ◽  
Hexane Extraction ◽  
Higher Plant ◽  
Major Site ◽  
Haem Biosynthesis

Ferrochelatase is the terminal enzyme of haem biosynthesis, catalysing the insertion of ferrous iron into the macrocycle of protoporphyrin IX, the last common intermediate of haem and chlorophyll synthesis. Its activity has been reported in both plastids and mitochondria of higher plants, but the relative amounts of the enzyme in the two organelles are unknown. Ferrochelatase is difficult to assay since ferrous iron requires strict anaerobic conditions to prevent oxidation, and in photosynthetic tissues chlorophyll interferes with the quantification of the product. Accordingly, we developed a sensitive fluorimetric assay for ferrochelatase that employs Co2+ and deuteroporphyrin in place of the natural substrates, and measures the decrease in deuteroporphyrin fluorescence. A hexane-extraction step to remove chlorophyll is included for green tissue. The assay is linear over a range of chloroplast protein concentrations, with an average specific activity of 0.68nmol·min−1·mg of protein−1, the highest yet reported. The corresponding value for mitochondria is 0.19nmol·min−1·mg of protein−1. The enzyme is inhibited by N-methylprotoporphyrin, with an estimated IC50 value of ≈ 1nM. Using this assay we have quantified ferrochelatase activity in plastids and mitochondria from green pea leaves, etiolated pea leaves and pea roots to determine the relative amounts in the two organelles. We found that, in all three tissues, greater than 90% of the activity was associated with plastids, but ferrochelatase was reproducibly detected in mitochondria, at levels greater than the contaminating plastid marker enzyme, and was latent. Our results indicate that plastids are the major site of haem biosynthesis in higher plant cells, but that mitochondria also have the capacity for haem production.

scholarly journals Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy

2021 ◽  
Vol 7 (9) ◽  
pp. 131
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
Yiannis Sanakis ◽  
George Mitrikas
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Spinacia Oleracea ◽  
Higher Plants ◽  
Correlation Spectroscopy ◽  
Oxygen Evolving Complex ◽  
Higher Plant ◽  
Proton Coupled Electron Transfer ◽  
S Oxidation

The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the oxygen evolving complex (OEC) of PSII. Two tyrosine residues D1-Tyr161 (YZ) and D2-Tyr160 (YD) are symmetrically placed in the two core subunits D1 and D2 and participate in proton coupled electron transfer reactions. YZ of PSII is near the OEC and mediates electron coupled proton transfer from Mn4Ca to the photooxidizable chlorophyll species P680+. YD does not directly interact with OEC, but is crucial for modulating the various S oxidation states of the OEC. In PSII from higher plants the environment of YD• radical has been extensively characterized only in spinach (Spinacia oleracea) Mn- depleted non functional PSII membranes. Here, we present a 2D-HYSCORE investigation in functional PSII of spinach to determine the electronic structure of YD• radical. The hyperfine couplings of the protons that interact with the YD• radical are determined and the relevant assignment is provided. A discussion on the similarities and differences between the present results and the results from studies performed in non functional PSII membranes from higher plants and PSII preparations from other organisms is given.

scholarly journals Purification and characterization of a thermostable ADP-glucose pyrophosphorylase from Thermus caldophilus GK-24

1996 ◽  
Vol 319 (3) ◽  
pp. 977-983 ◽  
Author(s):  
Jeong Heon KO ◽  
Cheorl Ho KIM ◽  
Dae-Sil LEE ◽  
Yu Sam KIM
Keyword(s):  
Molecular Mass ◽  
Specific Activity ◽  
Gel Filtration ◽  
Higher Plant ◽  
Sds Page ◽  
Thermus Caldophilus ◽  
Internal Peptide ◽  
Adp Glucose Pyrophosphorylase ◽  
Fructose 1,6 Bisphosphate

An extremely thermostable ADP-glucose pyrophosphorylase (AGPase) has been purified from Thermus caldophilus GK-24 to homogeneity by chromatographic methods, including gel filtration and ion-exchange and affinity chromatography. The specific activity of the enzyme was enriched 134.8-fold with a recovery of 10.5%. The purified enzyme was a single band by SDS/PAGE with a molecular mass of 52 kDa. The homotetrameric structure of the native enzyme was determined by gel filtration analysis, which showed a molecular mass of 230 kDa on a Superose-12 column, indicating that the structure of the enzyme is different from the heterotetrameric structures of higher-plant AGPases. The enzyme was most active at pH 6.0. The activity was maximal at 73–78 °C and its half-life was 30 min at 95 °C. Kinetic and regulatory properties were characterized. It was found that AGPase activity could be stimulated by a number of glycolytic intermediates. Fructose 6-phosphate, fructose 1,6-bisphosphate, phenylglyoxal and glucose 6-phosphate were effective activators, of which fructose 1,6-bisphosphate was the most effective. The enzyme was inhibited by phosphate, AMP or ADP. ATP and glucose 1-phosphate gave hyperbolic-shaped rate-concentration curves in the presence or absence of activator. A remarkable aspect of the amino acid composition was the existence of the hydrophobic and Ala+Gly residues. The N-terminal and internal peptide sequences were determined and compared with known sequences of various sources. It was apparently similar to those of AGPases from other bacterial and plant sources, suggesting that the enzymes are structurally related.

scholarly journals Genetic fine-structure of the GA-1 locus in the higher plant Arabidopsis thaliana (L.) Heynh

1983 ◽  
Vol 41 (1) ◽  
pp. 57-68 ◽  
Author(s):  
M. Koornneef ◽  
J. Van Eden ◽  
C. J. Hanhart ◽  
A. M. M. De Jongh
Keyword(s):  
Arabidopsis Thaliana ◽  
Fine Structure ◽  
Higher Plants ◽  
Wild Type ◽  
Higher Plant ◽  
Selfed Progeny ◽  
Intragenic Deletion ◽  
Genetic Length ◽  
Genetic Fine Structure ◽  
Half Diallel

SUMMARYNon-germinating gibberellin (GA) responsive mutants are a powerful tool to study genetic fine structure in higher plants. Nine alleles (EMS-and fast neutron-induced) of the ga-1 locus of Arabidopsis thaliana were tested in a complete half-diallel. No wild type ‘recombinants’ were found in the selfed progeny of 9 homoallelic combinations (in total 3 × 105 plants); in the progenies from the 36 selfed hetero allelics the wild type frequency ranged from zero to 6·6 × 10−4. These frequencies allowed the construction of an internally consistent map for five different sites representing eight alleles. The ninth allele covered three sites and thus behaved like an intragenic deletion. The estimate of the total genetic length of the ga-1 locus was 0·07 cM. The order of the sites was also clearly reflected by the association with proximal outside markers. On the assumption that wild type gametes predominantly arise from reciprocal events, it was shown that a cross-over within the ga-1 locus leads to positive interference in the adjacent region.The results are discussed with respect to the mutagen used, the frequencies found in other plant and Drosophila genes, and the possible occurrence of gene conversion.

The higher plant PII signal transduction protein: structure, function and properties

2007 ◽  
Vol 85 (6) ◽  
pp. 533-537 ◽  
Author(s):  
Greg B.G. Moorhead ◽  
Tony S. Ferrar ◽  
Yan M. Chen ◽  
Yutaka Mizuno ◽  
Catherine S. Smith ◽  
...  
Keyword(s):  
Higher Plants ◽  
Structural Features ◽  
Signaling Proteins ◽  
Higher Plant ◽  
Binding Partner ◽  
Signal Transduction Protein ◽  
Metabolic Sensor ◽  
Nitrogen Sensing ◽  
Over 40 Years

The PII carbon/nitrogen sensing protein was discovered in Escherichia coli (Migula 1895) Castellani and Chalmers 1919, over 40 years ago. Orthologues have been discovered in three kingdoms of life making it one of the most ancient and conserved signaling proteins known. Recent advances in the field have established its primary binding partner in plants as N-acetyl glutamate kinase and the crystal structure has revealed features unique to plants that likely contribute to its function in vivo. Here, we review the properties, function, and novel structural features of this chloroplast-localized metabolic sensor of higher plants.

Photoreduction of NADP+ in Photosystem II of Higher Plants: Requirement for Manganese

1992 ◽  
Vol 47 (1-2) ◽  
pp. 57-62 ◽  
Author(s):  
Suleyman I. Allakhverdiev ◽  
Vyacheslav V. Klimov
Keyword(s):  
Photosystem Ii ◽  
Higher Plants ◽  
Complete Removal ◽  
Reaction Centers ◽  
Higher Plant ◽  
Ps Ii ◽  
Alternate Pathway ◽  
Manganese Extraction ◽  
Quinone Acceptor ◽  
Reduced State

Abstract The effects of reversible manganese extraction on NADP+ photoreduction were studied with higher plant subchloroplast preparations of photosystem II (PS II). Under anaerobic conditions, when the reaction centers (RCs) of PS II are “closed” (i.e. in the state [P680 Pheo] QA), and in the presence of ferredoxin-ferredoxin-NADP+ reductase, NADP+ reduction is observed at a rate of 0.8 -1.1 nmol/mg × chlorophyll × h. After complete removal of manganese from PS II, the rate of NADP+ reduction is reduced 40 - 50-fold. Upon the addition of Mn at a concentration of approx. 4 Mn atoms per reaction center, the NADP+ reduction is restored up to 85 -90% of the initial value. When half of this amount of Mn is combined with about 40 times of the equivalent concentration of other divalent ions (Ca2+, Sr2+, Mg2+ etc.) the reaction is also reactivated. Dinoseb (10-6 m) an inhibitor of electron transfer in PS II prevents NADP+ photoreduction. It is concluded that under conditions when the first quinone acceptor, QA, is in its reduced state (QA-) electrons are transferred from reduced pheophytin (Pheo·̅) to NADP+, indicating that PS II can reduce NADP+ without the participation of PS I. On the basis of these and literature data, an alternate pathway for electron phototransfer in PS II reaction centers of higher plants is suggested. Some problems concerning the Z-scheme are discussed.

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