alcohol dehydrogenase/oryza sativa

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Distribution of Silicified Microstructures, Regulation of Cinnamyl Alcohol Dehydrogenase and Lodging Resistance in Silicon and Paclobutrazol Mediated Oryza sativa.

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Lodging is a phenomenon that affects most of the cereal crops including rice, Oryza sativa. This is due to the fragile nature of herbaceous plants whose stems are non-woody, thus affecting its ability to grow upright. Silicon (Si), a beneficial nutrient is often used to toughen and protect plants

The 5'-untranslated region of the Oryza sativa alcohol dehydrogenase gene functions as a translational enhancer in monocotyledonous plant cells.

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The 5'-untranslated region (5'-UTR) functions as a translational enhancer in monocotyledonous plant cells is necessary to express a foreign gene efficiently. Here, we show that the 5'-UTR of the rice alcohol dehydrogenase gene contributes to efficient translation in not only dicotyledonous plant

Comparative studies of isozymes in Oryza sativa, O. minuta, and their interspecific derivatives: evidence for homoeology and recombination.

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Enzyme electrophoresis was used to compare the isozyme phenotypes of Oryza sativa, IR31917 (AA genome), and two O. minuta accessions (Om 101089 and Om101141; BBCC genome) for ten enzyme systems. Between the two species, two systems were monomorphic (isocitrate dehydrogenase and alcohol

Inactivation of alcohol dehydrogenase in rice seedlings is related to a microsomal fatty acid alpha-oxidation system.

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The selective inactivation of alcohol dehydrogenase by the inactivator found in the microsomal fraction of rice (Oryza sativa) seedlings growing in air (Shimomura, S. & Beevers, H. (1983) Plant Physiol. 71, 736-741; 742-746) was further studied. This inactivation was found to be essentially

Alcohol dehydrogenase and an inactivator from rice seedlings.

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Alcohol dehydrogenase (ADH) was measured in the various organs of rice seedlings (Oryza sativa) growing in air. In extracts from ungerminated seeds, the ADH is stable, but in extracts from seedlings more than 2 days old the enzyme initially present loses activity in a time- and temperature-dependent

The 5'-untranslated region of the tobacco alcohol dehydrogenase gene functions as an effective translational enhancer in plant.

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The alcohol dehydrogenase gene (NtADH) was previously isolated from tobacco BY2 suspension cultured cell. Expression of this gene was dramatically increased only during the early stationary phase, and the 5'-untranslated region (5'-UTR) was hypothesized to be involved in the stimulatory effect at

Alcohol dehydrogenase inactivator from rice seedlings : properties and intracellular location.

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The alcohol dehydrogenase (ADH) inactivator from aerobically grown rice (Oryza sativa) coleoptiles was shown to be associated with membranes which were recovered in sucrose gradients at peak density 1.13 grams per cubic centimeter. When Mg(2+) was included in the gradient, the inactivator was

Investigating inducible short-chain alcohol dehydrogenases/reductases clarifies rice oryzalexin biosynthesis.

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Rice (Oryza sativa) produces a variety of labdane-related diterpenoids as phytoalexins and allelochemicals. The production of these important natural products has been partially elucidated. However, the oxidases responsible for production of the keto groups found in many of these diterpenoids have

Low-temperature accumulation of alcohol dehydrogenase-1 mRNA and protein activity in maize and rice seedlings.

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Low-temperature stress was shown to cause a rapid increase in steady-state levels of alcohol dehydrogenase-1 message (Adh1) and protein activity (ADH1) in maize (Zea mays) (B37N, A188) and rice (Oryza sativa) (Taipei 309, Calmochi 101) seedlings. Maize roots and rice shoots and roots from 7-day

GOLD HULL AND INTERNODE2 encodes a primarily multifunctional cinnamyl-alcohol dehydrogenase in rice.

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Lignin content and composition are two important agronomic traits for the utilization of agricultural residues. Rice (Oryza sativa) gold hull and internode phenotype is a classical morphological marker trait that has long been applied to breeding and genetics study. In this study, we have cloned the

Rice alcohol dehydrogenase 1 promotes survival and has a major impact on carbohydrate metabolism in the embryo and endosperm when seeds are germinated in partially oxygenated water.

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OBJECTIVE Rice (Oryza sativa) has the rare ability to germinate and elongate a coleoptile under oxygen-deficient conditions, which include both hypoxia and anoxia. It has previously been shown that ALCOHOL DEHYDROGENASE 1 (ADH1) is required for cell division and cell elongation in the coleoptile of

The cinnamyl alcohol dehydrogenase gene family in Populus: phylogeny, organization, and expression.

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BACKGROUND Lignin is a phenolic heteropolymer in secondary cell walls that plays a major role in the development of plants and their defense against pathogens. The biosynthesis of monolignols, which represent the main component of lignin involves many enzymes. The cinnamyl alcohol dehydrogenase

Chromosomal localization and genomic organization of α-amylase genes in rice (Oryza sativa L.).

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Genes for α-amylase, alcohol dehydrogenase, andEm, an ABA-regulated gene expressed late in embryogenesis, were localized on rice chromosomes by the analysis of primary trisomies. The validity of the mapping approach was confirmed usingAdh-1 as a control. TheAdh-1 gene has previously been assigned to

Rice Seed Germination Underwater: Morpho-Physiological Responses and the Bases of Differential Expression of Alcoholic Fermentation Enzymes.

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The water-, energy-, and labor-intensive system of transplanted puddled rice (Oryza sativa) is steadily being replaced by direct seeding due to the progressive scarcity of these resources. However, the alternate dry direct seeding leads to competition with weeds and poor establishment when soils are

Ethanol sensitivity of rice and oat coleoptiles.

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The ability to avoid the ethanol-induced injury was evaluated in rice (Oryza sativa L.) and oat (Avena sativa L.) coleoptiles. The growth of the rice and oat coleoptiles was inhibited by ethanol exogenously applied at concentrations greater than 200 and 30 mM, respectively. At 300 mM ethanol, oat

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