Topic
Aldehyde dehydrogenase
About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.
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TL;DR: An overview of the current knowledge of genetics, evolution, structure, enzymology, tissue distribution and regulation of mammalian aldehyde oxidases is provided.
Abstract: Mammalian aldehyde oxidases are a small group of proteins belonging to the larger family of molybdo-flavoenzymes along with xanthine oxidoreductase and other bacterial enzymes. The two general types of reactions catalyzed by aldehyde oxidases are the hydroxylation of heterocycles and the oxidation of aldehydes into the corresponding carboxylic acids. Different animal species are characterized by a different complement of aldehyde oxidase genes. Humans contain a single active gene, while marsupials and rodents are characterized by four such genes clustering at a short distance on the same chromosome. At present, little is known about the physiological relevance of aldehyde oxidases in humans and other mammals, although these enzymes are known to play a role in the metabolism of drugs and compounds of toxicological importance in the liver. The present article provides an overview of the current knowledge of genetics, evolution, structure, enzymology, tissue distribution and regulation of mammalian aldehyde oxidases.
171 citations
TL;DR: During the past 5 years considerable progress has been made in determining the number of gene loci coding for these enzymes and the tissue distribution of the enzymes, and the nature of the genetic variation in mitochondrial ALDH.
Abstract: During the past 5 years considerable progress has been made in the elucidation of the biochemical genetics of human alcohol dehydrogenases (ADH) and human aldehyde dehydrogenases (ALDH). In particular, progress has been made in determining the number of gene loci coding for these enzymes and the tissue distribution of the enzymes. In addition, a number of allelic variants of specific forms of alcohol and aldehyde dehydrogenases have been described. Studies have been done on different population groups to determine the frequencies of some of these variants. The relationship of the presence of variant forms of alcohol and aldehyde dehydrogenases to altered alcohol tolerance has been investigated. Efficient procedures for purifying alcohol and aldehyde dehydrogenases have been defined. As a result, detailed studies on the kinetics of separated isozymes and amino acid sequence determinations have been possible. To date, complete amino acid sequence data have been obtained for three ADH isozymes and one ALDH isozyme, while partial amino acid sequence data have been published on a second ALDH isozyme. Antibodies to specific forms of aldehyde dehydrogenase have been used to determine the nature of the genetic variation in mitochondrial ALDH.
170 citations
TL;DR: The sulfhydryl reagents dithiothreitol and reduced glutathione completely blocked the inhibition of AlDH by Angeli's salt and were able to partially restore activity to the nitroxyl-inhibited enzyme, the extent of reactivation being dependent on the pH at which the inactivation occurred.
168 citations
TL;DR: The data strongly suggest that genetic variation in both ADH and ALDH may influence drinking behavior and the risk of alcoholism developing through acetaldehyde formation, and suggest that the mutant ALDH2*2 gene may influence susceptibility to alcoholic cirrhosis.
168 citations
TL;DR: The efficiency of the recombinant strain(s) was improved by expressing DhaB and AldH in two compatible isopropyl‐thio‐β‐galactoside inducible plasmids along with glycerol dehydratase reactivase (GDR) and it was found that the changes in protein expression were associated with their enzymatic activity and balance.
Abstract: 3-Hydroxypropionic acid (3-HP) is a commercially valuable chemical with the potential to be a key building block for deriving many industrially important chemicals. However, its biological production has not been well documented. Our previous study demonstrated the feasibility of producing 3-HP from glycerol using the recombinant Escherichia coli SH254 expressing glycerol dehydratase (DhaB) and aldehyde dehydrogenase (AldH), and reported that an "imbalance between the two enzymes" and the "instability of the first enzyme DhaB" were the major factors limiting 3-HP production. In this study, the efficiency of the recombinant strain(s) was improved by expressing DhaB and AldH in two compatible isopropyl-thio-beta-galactoside (IPTG) inducible plasmids along with glycerol dehydratase reactivase (GDR). The expression levels of the two proteins were measured. It was found that the changes in protein expression were associated with their enzymatic activity and balance. While cloning an alternate aldehyde dehydrogenase (ALDH), alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH), instead of AldH, the recombinant E. coli SH-BGK1 showed the highest level of 3-HP production (2.8 g/L) under shake-flask conditions. When an aerobic fed-batch process was carried out under bioreactor conditions at pH 7.0, the recombinant SH-BGK1 produced 38.7 g 3-HP/L with an average yield of 35%. This article reports the highest level of 3-HP production from glycerol thus far.
168 citations