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homoserine/kukuruz
Veza se sprema u međuspremnik
Stranica 1 iz 17 rezultatima
Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family.
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Aspartate kinase (AK) and homoserine dehydrogenase (HSDH) are enzymes in the aspartate-derived amino acid biosynthetic pathway. Recent biochemical evidence indicates that an AK-HSDH bifunctional enzyme exists in maize (Zea mays L.). In this report, we characterize three genes that encode subunits of
Studies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays roots.
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Changes in Enzyme Regulation during Growth of Maize: I. Progressive Desensitization of Homoserine Dehydrogenase during Seedling Growth.
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The sensitivity of homoserine dehydrogenase (EC 1.1.1.3) to inhibition by the feed-back modifier, l-threonine, was examined in preparations derived from etiolated shoots, roots, and lightgrown tissues of Zea mays L. var. earliking. A progressive decrease in enzyme sensitivity was observed during
Changes in Enzyme Regulation during Growth of Maize: II. Relationships among Multiple Molecular Forms of Homoserine Dehydrogenase.
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The relative contribution of each of several forms of homoserine dehydrogenase (EC 1.1.1.3) to the total enzyme population in etiolated shoots and in roots of Zea mays L. var. earliking was examined by the use of gel filtration chromatography and disc gel electrophoresis. In enzyme preparations
Ligand-induced interconversions of maize homoserine dehydrogenase among different states.
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The threonine-sensitive homoserine dehydrogenase has been isolated and extensively purified from shoots of Zea mays L. var. earliking. This enzyme is shown to be hysteretic under certain conditions. Progress curves of the NAD-dependent reaction catalyzed by the maize enzyme can be characterized by
Differential Regulation of Maize Homoserine Dehydrogenase under Physiological Conditions.
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Homoserine dehydrogenase is associated with the multibranched pathway of amino acid biosynthesis originating with aspartic acid. Like most of the related pathway enzymes, this enzyme is localized in chloroplasts. The activity and regulatory properties of the threonine-sensitive isozyme of homoserine
Isolation and characterization of two homoserine dehydrogenases from maize suspension cultures.
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Homoserine dehydrogenase in unpurified extracts of maize (Zea mays L.) cell suspensions is inhibited 73% by the feedback regulator threonine; the remaining 27% of the total activity is not affected even by high concentrations of threonine. The threonine-resistant and threonine-sensitive homoserine
Quantitative estimates of the distribution of homoserine dehydrogenase isozymes in maize tissues.
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The low molecular weight threonine-resistant (class I) and the higher molecular weight threonine-sensitive (class II/III) isozymes of homoserine dehydrogenase (EC 1.1.1.3) isolated from Zea mays L. were shown to differ in stability during incubations in the presence of urea. Class II/III was
Effects of plant age and extraction conditions on the properties of homoserine dehydrogenase isolated from maize seedlings.
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Homoserine dehydrogenase (EC 1.1.1.3) was extracted from shoots of etiolated seedlings of Zea mays L. which had been grown for periods ranging from three to thirteen days. Both the amount of enzyme extracted and its regulatory properties, as measured by the sensitivity of the enzyme to inhibition by
Changes in Enzyme Regulation during Growth of Maize: III. Intracellular Localization of Homoserine Dehydrogenase in Chloroplasts.
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Extracts of leaf tissue of Zea mays L. seedlings were fractionated on nonlinear sucrose gradients to separate subcellular organelles. Homoserine dehydrogenase (EC 1.1.1.3) was identified in those fractions containing intact chloroplasts, as judged by the presence of chlorophyll and triosephosphate
Comparison of sensitive and desensitized forms of maize homoserine dehydrogenase.
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The properties of homoserine dehydrogenase (EC 1.1.1.3) isolated from shoots of young etiolated seedlings of Zea mays L. var. earliking can be reversibly altered by dialysis against an appropriate buffer. Treatment with 500 millimolar potassium phosphate buffer (pH 7.5) in the absence of l-threonine
Characterization of ligand-induced states of maize homoserine dehydrogenase.
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The threonine-sensitive homoserine dehydrogenase (L-homoserine: NAD(P)+ oxido-reductase), isolated from seedlings of Zea mays L., is characterized by variable kinetic and regulatory properties. Previous analysis of this enzyme suggested that it is capable of ligand-mediated interconversions among
Aspartate kinase 2. A candidate gene of a quantitative trait locus influencing free amino acid content in maize endosperm.
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The maize (Zea mays) Oh545o2 inbred accumulates an exceptionally high level of free amino acids, especially lysine (Lys), threonine (Thr), methionine, and iso-leucine. In a cross between Oh545o2 and Oh51Ao2, we identified several quantitative trait loci linked with this phenotype. One of these is on
Transcriptome-based analysis of the Pantoea stewartii quorum-sensing regulon and identification of EsaR direct targets.
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Pantoea stewartii subsp. stewartii is a proteobacterium that causes Stewart's wilt disease in corn plants. The bacteria form a biofilm in the xylem of infected plants and produce capsule that blocks water transport, eventually causing wilt. At low cell densities, the quorum-sensing (QS) regulatory
Pantoea stewartii subsp. stewartii: lessons learned from a xylem-dwelling pathogen of sweet corn.
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Pantoea stewartii subsp. stewartii is a Gram-negative enteric bacterium that primarily infects sweet corn. Studies of this bacterium have provided useful insight into how xylem-dwelling bacteria establish themselves and incite disease in their hosts. Pantoea stewartii subsp. stewartii is a
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