Toxic effects of sulfide come from a poisoning of a number of enzymes, especially cytochrome c oxidase, which catalyzes the terminal step in mitochondrial aerobic respiration. Despite this, some estuarine plants live in sulfide-rich sediments. We hypothesized estuarine and flooding-tolerant species might be more tolerant of sulfide compared to upland species, and this was tested by measures of ...

The alcohol dehydrogenase crystallized from horse liver contains 2 atoms of zinc per molecule and the activity of this enzyme is inhibited by metal-binding agents (1, 2). The inhibition of liver alcohol dehydrogenase by one of these agents, 1, IO-phenanthroline, differs from that which is observed when the alcohol dehydrogenase isolated from yeast is exposed to 1, lo-phenanthroline (3). The liv...

The thermostabilization of some enzymes by amidination with dimethylsuberimidate was surveyed. In the enzymes investigated, a moderate increase of thermostability in glucose oxidase and invertase, and prominent increase in lactate dehydrogenase, alcohol dehydrogenase and ascorbate oxidase were observed. The increase of thermostability by amidination was suggesting the synergism of the enhanceme...

Acetobacterium woodii formed ethanol as a fermentation product in addition to acetate when the phosphate concentration of the medium was between 0.2 and 8.4 mM. Considerable amounts of alanine were also found (2 to 11 mM). Supplementation with phosphate caused a shift to acetate as the only end product. Ethanol could also serve as a substrate for A. woodii. The fermentation yielded predominantl...

We have cloned and sequenced the alcohol dehydrogenase gene of the fission yeast Schizosaccharomyces pombe. The gene was isolated by transformation and complementation of a Saccharomyces cerevisiae strain which lacked functional alcohol dehydrogenase with an S. pombe gene bank constructed in the autonomously replicating yeast plasmid YEp13. Southern hybridization analysis indicates that S. pomb...

We present results showing that several species in the plant genus Leavenworthia, in the Brassica family, have three alcohol dehydrogenase loci, unlike Arabidopsis thaliana, which has only a single classical (class P) alcohol dehydrogenase locus. Based on a portion of the sequence, the alcohol dehydrogenase loci of Leavenworthia show about 92%-93% amino acid sequence identity to that of the A. ...

The alcohol dehydrogenase crystallized from horse liver contains 2 atoms of zinc per molecule and the activity of this enzyme is inhibited by metal-binding agents (1, 2). The inhibition of liver alcohol dehydrogenase by one of these agents, 1, IO-phenanthroline, differs from that which is observed when the alcohol dehydrogenase isolated from yeast is exposed to 1, lo-phenanthroline (3). The liv...

We describe an improved method for determination of alcohol dehydrogenase (EC 1.1.1.1) activity in 60 microL of human serum, based on conversion of ethanol to acetaldehyde with simultaneous reduction of NAD+ in glycine NaOH buffer (pH 9.0) at 37 degrees C in a centrifugal analyzer. The final concentration of NAD+ was 10 mmol/L and ethanol was 20 mmol/L. The dilution curve was linear with enzyme...

Objective To use the rs1229984 variant in the alcohol dehydrogenase 1B gene (ADH1B) as an instrument to investigate the causal role of alcohol in cardiovascular disease. Design Mendelian randomisation meta-analysis of 56 epidemiological

Escherichia coli AdhE has been reported to harbor three distinct enzymatic activities: alcohol dehydrogenase, acetaldehyde-CoA dehydrogenase, and pyruvate formate-lyase (PFL) deactivase. Herein we report on the cloning, expression, and purification of E. coli AdhE, and the re-investigation of its purported enzymatic activities. While both the alcohol dehydrogenase and acetaldehyde-CoA dehydroge...