Alcohol is eliminated from the body by various metabolic mechanisms. The primary enzymes involved are aldehyde dehydrogenase (ALDH), alcohol dehydrogenase (ADH), cytochrome P450 (CYP2E1), and catalase. Variations in the genes for these enzymes have been found to influence alcohol consumption, alcohol-related tissue damage, and alcohol dependence. The consequences of alcohol metabolism include o...

Two non-canonical amino acids (ncAAs) with bio-orthogonal reactive groups, namely, p-azido-L-phenylalanine (p-AzF) and p-propargyloxy-L-phenylalanine (p-PaF), were genetically inserted into an aldo-keto reductase (AKR) alcohol dehydrogenase (ADH), respectively, at...

Detailed drinking histories were taken in 38 patients in whom dilated cardiomyopathy was diagnosed by cardiac catheterisation and left ventricular biopsy. On the basis of the drinking history twenty patients were classified as being in an abstinent or light drinking group and eighteen patients as being in a heavy drinking group (daily alcohol intake in excess of 80 g or cumulative lifetime inta...

Exposure of freshly shed maize pollen to allyl alcohol vapors allows selective fertilization by mutant alcohol-dehydrogenase-negative grains. Wild-type pollen grains are killed by the enzymatic conversion of allyl alcohol to the highly toxic acrylaldehyde.

Several enzymes possess more than one specific function which can be selectively altered by various agents. For example, glutamic dehydrogenase oxidizes both alanine and glutamic acid (1) ; enzymic activity toward glutamic acid was inhibited by diethylstilbesterol while that toward alanine was stimulated by the same compound. The present communication describes studies on the alterations of the...

The origin of the fatty acid activation and formaldehyde dehydrogenase activity that distinguishes human class III alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) from all other alcohol dehydrogenases has been examined by site-directed mutagenesis of its Arg-115 residue. The Ala- and Asp-115 mutant proteins were expressed in Escherichia coli and purified by affinity chromatograp...

The secondary alcohol dehydrogenase is the enzyme of dehydration on the secondary alcohol. In 1965, Hardonkl' noted the similarity between the enzymes participating in the oxidative cleavage of the side chain of cholesterol as a precursor of steroid and secondary alcohol dehydrogenase. Using various secondary alcohols, the distribution of activity of the dehydrogenase in the human body was stud...

Pseudomonas sp. strain TW3 is able to oxidatively metabolize 4-nitrotoluene and toluene via a route analogous to the upper pathway of the TOL plasmids. We report the sequence and organization of five genes, ntnWCMAB*, which are very similar to and in the same order as the xyl operon of TOL plasmid pWW0 and present evidence that they encode enzymes which are expressed during growth on both 4-nit...

The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...

We have been working to develop an enzymatic assay for the alcohol 2-methyl-3-buten-2-ol (232-MB), which is produced and emitted by certain pines. To this end we have isolated the soil bacterium Pseudomonas putida MB-1, which uses 232-MB as a sole carbon source. Strain MB-1 contains inducible 3-methyl-2-buten-1-ol (321-MB) and 3-methyl-2-buten-1-al dehydrogenases, suggesting that 232-MB is meta...