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Molecular Aspects of the Activity and Inhibition of the FAD-Containing Monoamine Oxidases
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
All amine substrates are oxidized by MAO to the imine which is hydrolysed non-enzymically to the corresponding aldehyde (Fig. 10.1). Aldehydes are somewhat reactive molecules that can damage biological molecules by nucleophilic addition. In the cell, aldehyde dehydrogenase metabolizes the aldehyde to the carboxylic acid. The second product of MAO catalysis is hydrogen peroxide (H2O2). The toxic effect of MAO-generated H2O2 was clearly demonstrated for serotonin metabolism in heart (Pena-Silva et al., 2009). Decreased generation of H2O2 in the brain may contribute to the beneficial effects of selegiline.
Increasing Ethanol Tolerance in Industrially Important Ethanol Fermenting Organisms
Published in Ayerim Y. Hernández Almanza, Nagamani Balagurusamy, Héctor Ruiz Leza, Cristóbal N. Aguilar, Bioethanol, 2023
Kalyanasundaram Geetha Thanuja, Subburamu Karthikeyan
AdhE, a gene encodes for aldehyde dehydrogenase, the bifunctional and bidirectional enzyme. It is responsible for catalyzing two-terminal steps in the formation of ethanol: acetyl-CoA reduction to acetaldehyde by aldehyde dehydrogenase (ALDH) and reduction of acetaldehyde to ethanol by alcohol dehydrogenase (ADH) with two reduced electron donors, NADH, and NADPH. In C. thermocellum, the role of adhE is crucial and their deletion strain showed >90% activity loss of ALDH, ADH, and >95% reduction of ethanol production [67]. Point mutation resulted in the replacing certain amino acids at particular sites of ADH [3].
Thermostable Enzymes Produced by Recombinant Mesophilic and Thermophilic Bacteria
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Aldehyde dehydrogenase (ALDH) is a ubiquitous enzyme that participates in alcohol metabolism and biological oxidation of aldehyde compounds. Generally speaking, ALDH is very unstable because of spontaneous oxidation. Therefore, it is fairly difficult to analyze the enzyme’s characteristics.
Microbial and functional characterization of granulated sludge from full-scale UASB thermophilic reactor applied to sugarcane vinasse treatment
Published in Environmental Technology, 2022
Franciele Pereira Camargo, Isabel Kimiko Sakamoto, Tiago Palladino Delforno, Cédric Midoux, Iolanda Cristina Silveira Duarte, Edson Luiz Silva, Ariane Bize, Maria Bernadete Amâncio Varesche
The degradation pathways of several AD inhibitors were also considered. Only two KO related with the Limonene and pinene degradation pathway could be observed (Figure A.3), being the K00128 (0.049%) and K14731 (0.001%), the first one related only to (−)-S-limonene and the second one being related, in addition, to (+)-(R)-limonene degradation. The K00128, an aldehyde dehydrogenase (NAD+), is an enzyme with wide specificity, being related to several metabolic pathways, such as Glycolysis/Gluconeogenesis, Fatty acid degradation, Glycerolipid, Pyruvate and Aminoacids metabolisms, among others, catalyzing the conversion of an aldehyde to a carboxylate, as described before in the Equation (2). In the Limonene degradation pathway, it converts the perillyl aldehyde to perillyc acid.