Results 291 to 300 of about 157,588 (333)

Comparative proteomics analysis of root and nodule mitochondria of soybean

open access: yesPlant, Cell &Environment, EarlyView.
Abstract Legumes perform symbiotic nitrogen fixation through rhizobial bacteroids housed in specialised root nodules. The biochemical process is energy‐intensive and consumes a huge carbon source to generate sufficient reducing power. To maintain the symbiosis, malate is supplied by legume nodules to bacteroids as their major carbon and energy source ...
Wai‐Ching Sin   +4 more
wiley   +1 more source

Contextualized Metabolic Modelling Revealed Factors Affecting Isoflavone Accumulation in Soybean Seeds

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Isoflavones, secondary metabolites with numerous health benefits, are predominantly found in legume seeds, especially soybean; however, their contents in domesticated soybean seeds are highly variable. Wild soybeans are known for higher seed isoflavone contents than cultivars. Here we used experimental and modelling approaches on wild soybean (
Carolina A. Contador   +5 more
wiley   +1 more source

Diurnal Variations in Photochemical Energy Utilization and Osmotic Adjustments in Black Poplar Leaves Under Progressive Water Stress

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Drought limits the productivity of fast‐growing woody crops, although the metabolic adjustments conferring water stress tolerance remain poorly understood. We investigated the responses of Populus nigra seedlings to water stress by integrating daily physiological measurements and NMR metabolomic analyses.
Antonella Gori   +6 more
wiley   +1 more source

Unravelling the Significance of Phosphoenolpyruvate Carboxylase in Phosphate Starvation Responses

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Low phosphate availability is a major concern for agriculture. Plants develop a plethora of responses to improve phosphate acquisition, known as phosphate starvation responses (PSR). Among them, the induction of phosphoenolpyruvate carboxylase (PEPC) has been described in many plants. However, most studies have been conducted in the absence of
Jesús Pérez‐López   +10 more
wiley   +1 more source

Bivalent Histone Modifications Orchestrate Temporal Regulation of Glucosinolate Biosynthesis During Wound‐Induced Stress Responses in Arabidopsis

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Glucosinolates (GSLs) are secondary metabolites central to plant defence in the Brassicaceae family. While the role of histone modifications in developmental gene regulation is well studied, their function in stress‐induced secondary metabolism remains unclear.
Dasom Choi   +2 more
wiley   +1 more source
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Glutamate dehydrogenase of Tetrahymena

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract Glutamate dehydrogenase [ l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis . The activity with the four pyridine nucleotide substrates was catalyzed by a single enzyme as indicated by the
Kenneth Kemp   +2 more
openaire   +3 more sources

Studies of Glutamate Dehydrogenase

European Journal of Biochemistry, 1973
Specific interaction between α‐NADH and glutamate dehydrogenase is demonstrated by difference spectroscopy, circular dichroism and fluorescence measurements. Quantitative binding studies in the preparative ultracentrifuge yield six identical α‐NADH binding sites per oligomer with a dissociation constant of 20 μM.
Rudolf Koberstein   +2 more
openaire   +3 more sources

Glutamate dehydrogenase-malate dehydrogenase complex

Archives of Biochemistry and Biophysics, 1979
Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
Linda Lou Smith   +2 more
openaire   +3 more sources

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