نتایج جستجو برای: adh alcohol dehydrogenase

تعداد نتایج: 185772  

Journal: :Bioscience, biotechnology, and biochemistry 1997
D Tsuru N Oda Y Matsuo S Ishikawa K Ito T Yoshimoto

The role of cysteine residues for structure and function of formaldehyde dehydrogenase from Pseudomonas putida was analysed by amino acid sequence comparison, homology-based structure modeling, site-directed mutagenesis, and chemical modification. Five out of seven cysteine residues found in the enzyme were concluded to coordinate with an active site zinc (Cys-46) and structural zinc atoms (Cys...

2010
Zaijun Zhang Sha Li Jie Jiang Pei Yu Jing Liang Yuqiang Wang

BACKGROUND Radix Puerariae is used in Chinese medicine to treat alcohol addiction and intoxication. The present study investigates the effects of Flos puerariae lobatae water extract (FPE) and its active ingredient puerarin on alcoholism using rodent models. METHODS Alcoholic animals were given FPE or puerarin by oral intubation prior or after alcohol treatment. The loss of righting reflex (L...

Journal: :Alcoholism, clinical and experimental research 2005
Victor Hesselbrock Susumu Higuchi Michael Soyka

This article presents the proceedings of a symposia held at the International Society for Biomedical Research on Alcoholism Congress in Mannheim, Germany, in October, 2004 and focused on recent developments in alcohol-related phenotypes from three different research groups. The first presentation focused on the possible contribution of polymorphisms of alcohol dehydrogenase (ADH) and aldehyde d...

Journal: :Molecular biology and evolution 1991
M S Thomson J W Jacobson C C Laurie

Alcohol dehydrogenase (ADH) gene expression was analyzed in Drosophila melanogaster and its sibling species D. simulans. The levels of ADH activity, ADH-cross-reacting material (CRM), and ADH-mRNA were analyzed for several strains of each species, which derive from diverse geographic locations around the world. There is considerable quantitative variation in ADH activity, CRM level, and RNA lev...

Journal: :Genetics 1986
R G Rowan M D Brennan W J Dickinson

The organization of the gene coding for alcohol dehydrogenase (Adh) in Drosophila affinidisjuncta has been determined by physically mapping Adh RNA transcripts to cloned genomic DNA. Two distinct transcript types accumulate with developmental specificity. Because only a single genomic Adh locus is detected in D. affinidisjuncta, and since all Adh transcripts appear to be identical except at the...

2011
Indira Priyadarshini Pathuri Ines E. Reitberger Ralph Hückelhoven Reinhard K. Proels

Plant primary energy metabolism is profoundly reorganized under biotic stress conditions and there is increasing evidence for a role for the fermentative pathway in biotic interactions. However, the mechanisms regulating metabolic reprogramming are not well understood despite its critical function in the biotic stress response. Here the function of alcohol dehydrogenase (ADH) in the interaction...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1990
C C Laurie E M Heath J W Jacobson M S Thomson

Drosophila melanogaster and its sibling species, Drosophila simulans, differ in expression of the enzyme alcohol dehydrogenase (ADH). Adult melanogaster flies that are homozygous for the Slow allozyme have approximately twice the level of ADH activity and crossreacting material as simulans adults. There is no corresponding difference in ADH mRNA, however, so this difference in ADH protein level...

Journal: :Evolution; international journal of organic evolution 2008
James D Fry Kathy Donlon Molly Saweikis

Clinally varying traits in Drosophila melanogaster provide good opportunities for elucidating the genetic basis of adaptation. Resistance to ethanol, a natural component of D. melanogaster's breeding sites, increases with latitude on multiple continents, indicating that the trait is under selection. Although the well-studied Alcohol dehydrogenase (Adh) polymorphism makes a contribution to the c...

Journal: :Genetics 1987
S W Schaeffer C F Aquadro

The alcohol dehydrogenase (Adh) locus (ADH; alcohol: NAD+ oxidoreductase, EC 1.1.1.1) of Drosophila pseudoobscura was cloned and sequenced. Forty-five percent of the "effectively silent sites" have changed between Adh in D. pseudoobscura of the obscura species group and the homologous DNA sequence in D. mauritiana, the latter representing the melanogaster species group. The untranslated leader ...

2015
Saúl Gómez-Manzo José E. Escamilla Abigail González-Valdez Gabriel López-Velázquez América Vanoye-Carlo Jaime Marcial-Quino Ignacio de la Mora-de la Mora Itzhel Garcia-Torres Sergio Enríquez-Flores Martha Lucinda Contreras-Zentella Roberto Arreguín-Espinosa Peter M. H. Kroneck Martha Elena Sosa-Torres

Gluconacetobacter diazotrophicus is a N2-fixing bacterium endophyte from sugar cane. The oxidation of ethanol to acetic acid of this organism takes place in the periplasmic space, and this reaction is catalyzed by two membrane-bound enzymes complexes: the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase (ALDH). We present strong evidence showing that the well-known membrane-bound Alco...

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