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Vitamin E levels in soybean (Glycine max (L.) Merr.) expressing a p-hydroxyphenylpyruvate gene from oat (Avena sativa L.).
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The enzyme p-hydroxyphenylpyruvate dioxygenase (HPPD) is ubiquitous in plants and functions in the tyrosine catabolic pathway, resulting in the formation of homogentisate. Homogentisate is the aromatic precursor of all plastoquinones and tocochromanols, including tocopherols and tocotrienols.
Redox regulation of a soybean tyrosine-specific protein phosphatase.
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Plant protein tyrosine phosphatases (PTPs) are important in regulating cellular responses to redox change through their reversible inactivation under oxidative conditions. Studies on the soybean (Glycine max) GmPTP have shown that, compared with its mammalian counterparts, the plant enzyme is
L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers
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Mucuna pruriens L., commonly known as velvetbean or cow-itch, is a self-pollinated tropical legume of the family Fabaceae, known for its medicinal properties. The active principle L-DOPA extracted from the plant is a potent drug used in the treatment of Parkinson's disease. Although, it is
Characteristics of Modified Leghemoglobins Isolated from Soybean (Glycine max Merr.) Root Nodules.
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Hemoprotein derivatives of an abundant soybean (Glycine max Merr.) root nodule leghemoglobin, Lba, were studied for their modified spectral characteristics and physical properties. Three modified hemoprotein derivatives of Lba (Lbam1, Lbam2, and Lbam3) were purified by preparative isoelectric
A Pod Leakage Technique for Phloem Translocation Studies in Soybean (Glycine max [L.] Merr.).
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Radioactive photosynthetic assimilates, translocated to a soybean (Glycine max [L.] Merr. ;Fiskeby V') pod can be measured directly by excising the stylar tip of the pod under 20 mm ethylenediaminetetraacetate solution (pH 7.0) and allowing the material to leak into the solution. Pods at the source
Reaction Mechanism of Prephenate Dehydrogenase from the Alternative Tyrosine Biosynthesis Pathway in Plants.
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Unlike metazoans, plants, bacteria, and fungi retain the enzymatic machinery necessary to synthesize the three aromatic amino acids l-phenylalanine, l-tyrosine, and l-tryptophan de novo. In legumes, such as soybean, alfalfa, and common bean, prephenate dehydrogenase (PDH) catalyzes the
Phenylalanine is required to promote specific developmental responses and prevents cellular damage in response to ultraviolet light in soybean (Glycine max) during the seed-to-seedling transition.
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UV-radiation elicits a suite of developmental (photomorphogenic) and protective responses in plants, but responses early post-germination have received little attention, particularly in intensively bred plants of economic importance. We examined germination, hypocotyl elongation, leaf pubescence and
Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes.
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L-Tyrosine (Tyr) and its plant-derived natural products are essential in both plants and humans. In plants, Tyr is generally assumed to be synthesized in the plastids via arogenate dehydrogenase (TyrA(a), also known also ADH), which is strictly inhibited by L-Tyr. Using phylogenetic and expression
Acid phosphatase activities during the germination of Glycine max seeds.
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In this paper, we describe a study concerning the determination of some characteristics of soybean seedlings and the detection of acid phosphatase activities towards different substrates during the germination. Enzyme activities with p-nitrophenylphosphate (pNPP) and inorganic pyrophosphate (PPi) as
A novel lipoxygenase in pea roots. Its function in wounding and biotic stress.
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The genome of pea (Pisum sativum) contains genes encoding a family of distinct lipoxygenases (LOX). Among these, LOXN2 showed eight exons encoding a 93.7-kD enzyme, harboring two C-terminal deletions and an unusual arginine/threonine-tyrosine motif in the domain considered to control the substrate
Expression of a feedback insensitive anthranilate synthase gene from tobacco increases free tryptophan in soybean plants.
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Soybean [Glycine max (L.) Merr.] embryogenic cultures were transformed by particle bombardment with the feedback-insensitive tobacco anthranilate synthase (AS) gene ASA2 driven by the CaMV 35S promoter and selected using hph as the selectable marker gene. Only one of eight regenerated lines that set
Variation of the amino acid content of Arabidopsis seeds by expressing soybean aspartate aminotransferase gene.
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We have increased the contents of several amino acids in the seeds of Arabidopsis thaliana by introduction of aspartate aminotransferase (AAT), an enzyme of the aspartate biosynthetic pathway. mRNA was prepared from one-week-old seedlings of Glycine max cv. enrei and the cDNA encoding AAT5 was
Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom.
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Extensins (EXTs) are a family of plant cell wall hydroxyproline-rich glycoproteins (HRGPs) that are implicated to play important roles in plant growth, development, and defense. Structurally, EXTs are characterized by the repeated occurrence of serine (Ser) followed by three to five prolines (Pro)
Circular dichroism studies on the effects of sodium dodecyl sulfate on the conformation of some phytohemagglutinins.
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Conformation and conformational transitions of phytohemagglutinins (lectins) from Arachis hypogaea (peanut), Lens culinaris (lentil), Glycine max (soybean), and Ricinus communis (castor bean) were studied by the circular dichroism probe. The lectins were found to possess a high amount of the pleated
Circular dichroism tests on the effect of alkali on conformation of lectins.
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The structural properties of eight lectins (agglutinins) were studied by the circular dichroism (CD) probe. The lectin from Maclura pomifera (osage orange seed) exhibited in the far-ultraviolet spectral zone a positive CD band centered at 201 nm, whereas the other lectins had positive bands at
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