Oxidoreductases aldehyde reductase

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

Kelly VP, Ellis EM, Manson MM, Chanas SA, Moffat GJ. 2000. Chemopreven-tion of aflatoxin Bl hepatocarcinogen-esis by coumarin, a natural benzopyrene that is a potent inducer of aflatoxin Bl-aldehyde reductase, the glutathione Y-transferase A5 and PI subunits, and NAD(P)H quinone oxidoreductase in rat liver. Cancer Res. 60 957-69... 

Enzymes categorized as aldehyde reductases include alcohol dehydrogenase (NADP aldehyde reductase [NADPH] alcoholrNADP oxidoreductase EC 1.1,1,2), aldehyde reductase [alditol NAD(P ) 1-oxidoreductase aldose reductase EC 1.1.1.211, and many others... 

Until now, several oxidoreductases or microorganisms have been used in the preparation of chiral alcohols including NAD -dependent alcohol dehydrogenases (ADHs) from yeast and horse liver [11] (EC 1.1.1.1), Candida parapsilosis [12] and Pseudomonas sp. [13], and NADP -dependent ADHs from yeast [14], Thermoanaer-obium brockii [15] and Lactobacillus kefir [16], aldehyde reductases from Sporobolo-myces salmonicolor (EC 1.1.1.2) [17] and Penicillium citrinum (EC 1.1.1.21) [18], and carbonyl reductase (EC 1.1.1.184) from Candida magnoliae [19]. Our research group has reported an efficient method for producing both enantiomers of chiral alcohols... 

He A, T Li, L Daniels, I Fotheringham, JPN Rosazza (2004) Nocardia sp. carboxylic acid reductase cloning, expression, and characterization of a new aldehyde oxidoreductase family. Appl Environ Microbiol 70 1874-1881. 

The aldehyde ferredoxin oxidoreductase from the hyperthermophile Pyrococcus furiosus was the first molybdopterin-dependent enzyme for which a three-dimensional structure became available.683,684 The tungstoenzyme resembles that of the related molybdo-enzyme (Fig. 16-31). A similar ferredoxin-dependent enzyme reduces glyceraldehyde-3-phosphate.685 Another member of the tungstoenzyme aldehyde oxidoreductase family is carboxylic acid reductase, an enzyme found in certain acetogenic clostridia. It is able to use reduced ferredoxin to convert unactivated carboxylic acids into aldehydes, even though E° for the acetaldehyde/acetate couple is -0.58 V.686... 

As with xanthine oxidase, the sulfido ligand of the active form of aldehyde oxidoreductase is readily replaced by an oxido ligand to yield a cofactor with a structure that resembles that of oxidized sulfite oxidase and assimilatoiy nitrate reductase. Both x-ray and EXAFS data are available for the bis(oxido) form, and, with the exception of the oxido replaced sulfido ligand, few changes are obvious in the overall structure of the oxidized form of the desulfo cofactor. Upon reduction of the enzyme the oxido ligand is presumably reduced to hydroxido, an observation that is supported by EPR data for the Mov state. 

Figure 16. Consensus oxidized active-site structures of the xanthine oxidase (XO), sulfite oxidase (SO), and DMSO reductase (DMSOR), and aldehyde oxidoreductase (AOR) families of mononuclear molybdenum and tungsten enzymes and the structure of the common ppd cofactor (41, 42). The question mark in the AOR structure indicates uncertainty in the presence of a coordinated water molecule.

Numerous oxo-molybdo-bis(dithiolene) and oxo-tungsto-bis(dithiolene) complexes have been synthesized and characterized as potential structural analogues of the active sites of the dimethyl sulfoxide reductase (DMSOR) and aldehyde oxidoreductase (AOR) families of mononuclear Mo and W enzymes [see Fig. 16 and Chapter 10 in this volume (50)]. The available IR and Raman data for the Mo and W complexes are summarized in Tables VII and VIII,... 

Aldehyde ferredoxin oxidoreductase Benzene-1,2-dithiolate Biotin sulfoxide reductase Density functional theory... 

A few representative Mo enzymes are listed in Table 18-C-6. Note that most have very high molecular weights, and this has delayed structure determinations. In the case of DMSO-reductase, however, the lower molecular weight has made possible a structure determination. The Mo site is found to be as shown in 18-C-XXVII. In a tungsten-containing enzyme, ferredoxin aldehyde oxidoreductase, the metal site is as shown in 18-C-XXVIII. 

Total mass. Per subunit. Structural data can be obtained from the Brookhaven Protein Data Bank (PDB) at http //www.rcsb.org/pdb. Other Mo-MPT enzyme PDB codes include Hydrogenophagapseudoflava CO dehydrogenase, IFFV Desulfovibrio desulfuricans aldehyde oxidoreductase, IDGJ Rhodobacter capsulatus DMSO reductase, 4DMR R. sphaeroides nitrate reductase (dissimilatory), lOGY D. 

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