Salete Aparecida Gaziola

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Quality protein maize (QPM) varieties have been produced by the introduction of opaque-2 modifier genes. Two QPM varieties, BR451 and BR473, a wild type and an opaque-2 variety, have been used to study key enzymes controlling lysine metabolism in the endosperm during development. Aspartate kinase and homoserine dehydrogenase enzymes, which are involved in(More)
In plant, the catabolism of lysine has only been studied in some detail in maize. The enzymes lysine 2-oxoglutarate reductase (also known as lysine alpha-ketoglutarate reductase; LOR) and saccharopine dehydrogenase (SDH), which convert lysine into saccharopine, and saccharopine into glutamic acid and 2-aminoadipate 6-semialdehyde, respectively, were(More)
Two high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine,(More)
Lysine is an essential amino acid synthesized in plants via the aspartic acid pathway. The catabolism of lysine is performed by the action of two consecutive enzymes, lysine 2-oxoglutarate reductase (LOR, EC and saccharopine dehydrogenase (SDH, EC The final soluble lysine concentration in cereal seeds is controlled by both synthesis and(More)
The capacity of two maize opaque endosperm mutants (o1 and o2) and two floury (fl1 and fl2) to accumulate lysine in the seed in relation to their wild type counterparts Oh43+ was examined. The highest total lysine content was 3.78% in the o2 mutant and the lowest 1.87% in fl1, as compared with the wild type (1.49%). For soluble lysine, o2 exhibited over a(More)
 Lysine is catabolyzed by the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase (LOR-SDH) in both animals and plants. LOR condenses lysine and 2-oxoglutarate into saccharopine, using NADPH as cofactor and SDH converts saccharopine into α-aminoadipate δ-semialdehyde and glutamic acid, using NAD as cofactor. The distribution(More)
The grain proteins of barley are deficient in lysine and threonine due to their low concentrations in the major storage protein class, the hordeins, especially in the C-hordein subgroup. Previously produced antisense C-hordein transgenic barley lines have an improved amino acid composition, with increased lysine, methionine and threonine contents. The(More)
Hordeins are the major storage proteins in barley grains and are responsible for their low nutritional quality. Previously, antisense C-hordein barley lines were generated and were shown to contain a more balanced amino acid composition and an altered storage protein profile. In the present study, a proteomic approach that combined two-dimensional gel(More)
Both the scientific community and society have shown interest in improving the content of amino acids, carbohydrates and mineral nutrients in maize because it represents an important staple food in many developing countries. Earlier studies demonstrated that the treatment of seeds using ascorbic acid (AsA-seed priming) enhanced soluble carbohydrates,(More)
Storage of recalcitrant seeds leads to the initiation of subcellular damage or to the initiation of germination process, and both may result in viability loss. This study aimed to elucidate the biochemical basis of embryos survival of Araucaria angustifolia recalcitrant seeds during storage. After harvesting, seeds were stored at ambient conditions (without(More)
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