Acetaldehyde Dehydrogenase
Mostrando 1-12 de 90 artigos, teses e dissertações.
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1. Avaliação de polimorfismos em genes de metabolismo do etanol e gene de reparo do DNA em pacientes portadores de câncer de boca / Evaluation of polymorphisms in genes of ethanol metabolism and DNA repair gene in patients with oral cancer
O carcinoma epidermóide é uma neoplasia que pode ter origem do revestimento mucoso de vários sítios das vias aerodigestivas superiores, sendo a língua o sítio primário com maior incidência. Entre os fatores de risco para a doença estão a idade, as mutações genômicas, o hábito tabagista e principalmente o consumo de etanol. O etanol é considera
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 30/08/2012
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2. Genes de metabolização do álcool e o risco de câncer de cabeça e pescoço / Alcohol metabolizing genes and the risk of head and neck cancer
Garcia, S.M.N. Alcohol metabolizing genes and the risk of head and neck cancer. 2009. Dissertação (Mestrado)- Faculdade de Medicina, Universidade de São Paulo, São Paulo. The incidence of head and neck cancer (HNC) has increased substantially in the last years, including in Brazil. This increase is associated to alcohol and tobacco consumption, but genet
Publicado em: 2009
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3. Development of automatic procedures for the determination of ethanol, glycerol and tartaric acid in wine using multicommutation in flow. / Desenvolvimento de procedimentos automáticos para determinação de etanol, glicerol e ácido tartárico em vinho empregando multicomutação em fluxo.
In the present work, flow systems for the determination of ethanol, glycerol and tartaric acid in wine without previous sample treatment are described. The flow system were based on multicommutation and controlled by microcomputer allowing that the analytic procedures were accomplished automatically without the intervention of the operator. For ethanol deter
Publicado em: 2004
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4. Ethanol dehydrogenase activity in starter cultures for yoghurt under cold storage conditions / Atividade de etanol desidrogenase durante a estocagem em culturas usadas na produção de iogurte
Alcohol dehydrogenase, ADH, activity was investigated in Streptococcus thermophilus NCDO 1968, Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842, Lactobacillus acidophilus ATCC 4356, and the probiotic strain Lactobacillus delbrueckii UFV H2b20, after growth at 37C for 12 hours, and storage at 4C for 21 days. L. delbrueckii subsp. bulgaricus and L. acido
Publicado em: 2003
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5. Acetaldehyde coenzyme A dehydrogenase of Escherichia coli.
Mutants of Escherichia coli (adh) in which alcohol dehydrogenase is derepressed under aerobic conditions were also found to overproduce acetaldehyde coenzyme a dehydrogenase. However, acetaldehyde coenzyme A dehydrogenase was induced by ethanol or acetaldehyde and subject to strong catabolite repression, whereas alcohol dehydrogenase was little affected by t
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6. Metabolism of acetylene by Nocardia rhodochrous.
A Nocardia rhodochrous strain capable of utilizing acetylene as its sole source of carbon and energy exhibited slow growth on low concentrations of acetaldehyde. Resting cells incubated with acetylene formed a product identified as acetaldehyde, but attempts to demonstrate acetylene hydrase activity in cell-free extracts were unsuccessful. Acetaldehyde dehyd
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7. Biochemical basis of mitochondrial acetaldehyde dismutation in Saccharomyces cerevisiae.
As reported previously, Saccharomyces cerevisiae cells deficient in all four known genes coding for alcohol dehydrogenases (ADH1 through ADH4) produce considerable amounts of ethanol during aerobic growth on glucose. It has been suggested that ethanol production in such adh0 cells is a corollary of acetaldehyde dismutation in mitochondria. This could be subs
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8. Regulation of Product Formation in Bacteroides xylanolyticus X5-1 by Interspecies Electron Transfer
Bacteroides xylanolyticus X5-1 was grown in pure culture and in mixed culture with Methanospirillum hungatei JF-1 under xylose limitation in the chemostat. In the pure culture, ethanol, acetate, CO2, and hydrogen were the products. In the mixed culture, acetate, CO2, and presumably hydrogen were the only products formed by B. xylanolyticus X5-1. The biomass
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9. Absence of 5-Hydroxy-4-Ketohexanoate and the α-Ketoglutarate Dehydrogenase Complex in Mutants of Saccharomyces oviformis Incapable of Growing on Ethanol
The roles of the enzyme which forms 5-hydroxy-4-ketohexanoate (HKH) and of related enzymes in the metabolism of ethanol were studied in Saccharomyces oviformis WH92 and its mutants, which grew poorly or not at all on ethanol. The strains, which did not grow on ethanol, did not form HKH from α-ketoglutarate and acetaldehyde enzymatically and were also devoid
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10. Production of Acetaldehyde by Zymomonas mobilis
Mutants of Zymomonas mobilis were selected for decreased alcohol dehydrogenase activity by using consecutively higher concentrations of allyl alcohol. A mutant selected by using 100 mM allyl alcohol produced acetaldehyde at a level of 4.08 g/liter when the organism was grown in aerated batch cultures on a medium containing 4.0% (wt/wt) glucose. On the basis
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11. The Mitochondrial Alcohol Dehydrogenase Adh3p Is Involved in a Redox Shuttle in Saccharomyces cerevisiae
NDI1 is the unique gene encoding the internal mitochondrial NADH dehydrogenase of Saccharomyces cerevisiae. The enzyme catalyzes the transfer of electrons from intramitochondrial NADH to ubiquinone. Surprisingly, NDI1 is not essential for respiratory growth. Here we demonstrate that this is due to in vivo activity of an ethanol-acetaldehyde redox shuttle, wh
American Society for Microbiology.
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12. Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase.
Mutants of Escherichia coli resistant to allyl alcohol were selected. Such mutants were found to lack alcohol dehydrogenase. In addition, mutants with temperature-sensitive alcohol dehydrogenase activity were obtained. These mutations, designated adhE, are all located at the previously described adh regulatory locus. Most adhE mutants were also defective in