Oxidoreductases aldehyde dehydrogenase

Enzymes Oxidoreductases Aldehyde dehydrogenase Disulfiram (inhibitor)... 

The aldehyde dehydrogenases are members of a superfamily of pyridine nucleotide [NAD(P)+]-dependant oxidoreductases that catalyze the oxidation of aldehydes to... 

PHYSICAL ORGANIC CHEMISTRY NOMENCLATURE ALDEHYDE DEHYDROGENASE ALDEHYDE HYDRATION ALDEHYDE OXIDASE ALDEHYDE OXIDOREDUCTASE ALDOSE REDUCTASE Aldehyde reduction to alcohols, BOROHYDRIDE REDUCTION ALDOLASE Aldolase reduction,... 

Fatty aldehyde dehydrogenase (FALDH) and Fatty alcohohNAD oxidoreductase (FAO) Sjogren Larsson syndrome... 

FALDH Fatty aldehyde dehydrogenase and fatty alcohol NAD-oxidoreducease phosphate oxidoreductase... 

The bioconversion of eugenol and ferulic acid to vanillin was first characterised in Pseudomonas fluorescens (Scheme 26.4) [36, 37]. However, an enzyme of the pathway, vanillin NAD+ oxidoreductase, catalysed the removal of vanillin from the medium through the formation of vanillic acid [38]. Deletion of the oxidoreductase was, however, only partially successful, largely because vanillin is also the substrate of coniferyl aldehyde dehydrogenase, an enzyme of the eugenol degradative pathway present in Pseudomonas sp. [39]. 

Sanchez LB (1998) Aldehyde dehydrogenase (CoA-acetylating) and the mechanism of ethanol formation in the amitochondriate protist, Giardia lamblia. Arch Biochem Biophys 354 57-64 Saraste M (1999) Oxidative phosphorylation at the fin de siecle. Science 283 1488-1493 Saruta F, Kuramochi T, Nakamura K, Takamiya S, Yu Y, Aoki T, Sekimizu K, Kojima S, Kita K (1995) Stage-specific isoforms of complex II (succinate-ubiquinone oxidoreductase) in mitochondria from the parasitic nematode, Ascaris suum. J Biol Chem 270 928-932 Scheffler I (1999) Mitochondria. Wiley-Liss, New York... 

Aldehyde dehydrogenases [AEDHs alde-hyde NAD(P) oxidoreductases EC 1.2.1.3 and EC 1.2.1.51 exist in multiple forms in the cytosol, mitochondria, and microsomes of various mammalian tissues. It has been proposed that AEDHs form a superfamily of related enzymes consisting of class 1 AEDHs (cytosolic), class 2 AEDHs (mitochondrial), and class 3 AEDHs (tumor-associated and other isozymes). In all three major classes, constitutive and inducible isozymes exist. In a proposed nomenclature system, the human AEDHs are designated as lAl, 1A6, IBl, 2, 3A1, 3A2, 3B1, 3B2, 4A1, 5A1, 6A1, 7A1, 8A1, and 9A1 (33-35). 

Fatty alcohohNAD oxidoreductase is a complex enzyme which consists of two separate proteins that sequentially catalyze the oxidation of fatty alcohol to fatty aldehyde and to fatty acid that is to say a fatty alcohol dehydrogenase and a fatty aldehyde dehydrogenase (FALDH) activity. Sjogren-Larsson cells were selectively deficient in the FALDH component and had normal activity of fatty alcohol dehydrogenase. Intact fibroblast oxidized octadecanol to fatty acid at <10% of the normal rate but oxidized octadecanal normally confirming that FALDH is specifically affected (Rizzo and Craft, 1991). 

Rizzo W.B., Craft D.A., Sjogren-Larsson syndrome. Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol NAD+ oxidoreductase in cultured fibroblasts, The Journal of clinical investigation 88 (1991) 1643-1648. 

Besides the monooxygenases discussed above, a number of other oxidoreductases can oxidize xenobiotics. These enzymes are mostly but not exclusively nonmicrosomal, being present in the cytosol or mitochondria of the liver and extrahepatic tissues. The list includes alcohol dehydrogenases, aldehyde dehydrogenases, dihydrodiol dehydrogenases, haemoglobin, monoamine oxidases, xanthine oxidase and aldehyde oxidase. Some of these enzyme systems are discussed below. 

Oxidoreductases NADorNADP Alcoholdehydrogenases Aldehyde dehydrogenases 2-enoate reductase Amino acid dehydrogenase Aromatic dioxygenase Methane monooxygenase... 

Hydrolases identified include amylases, lipases, esterases, proteinases and phosphatases. Proteinase inhibitors have also been found. Important oxidoreductases in milk are aldehyde dehydrogenase (xanthine oxidase), lactoperoxidase and catalase. A general idea of the occurrence and localization of enzymes in boving milk is given in Table 10.24... 

The possibility of isolating the components of the two above-reported coupled reactions offered a new analytical way to determine NADH, FMN, aldehydes, or oxygen. Methods based on NAD(P)H determination have been available for some time and NAD(H)-, NADP(H)-, NAD(P)-dependent enzymes and their substrates were measured by using bioluminescent assays. The high redox potential of the couple NAD+/NADH tended to limit the applications of dehydrogenases in coupled assay, as equilibrium does not favor NADH formation. Moreover, the various reagents are not all perfectly stable in all conditions. Examples of the enzymes and substrates determined by using the bacterial luciferase and the NAD(P)H FMN oxidoreductase, also coupled to other enzymes, are listed in Table 5. 

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