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Aldose
About: Aldose is a research topic. Over the lifetime, 1270 publications have been published within this topic receiving 27197 citations. The topic is also known as: aldoses.
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TL;DR: The ARII protein was overproduced in Escherichia coli about 2,000-fold compared to the production in the original yeast cells, and the enzyme expressed in E. coli was purified to homogeneity and had the same catalytic properties as ARII purified from S. salmonicolor.
Abstract: Aldehyde reductase (EC 1.1.1.2), aldose reductase (EC 1.1.1.21), and carbonyl reductase (EC 1.1.1.184) catalyze NADPH-dependent reduction of a variety of carbonyl compounds and are widely distributed in mammalian and plant tissues. These enzymes are members of the aldo-keto reductase superfamily (4, 8); however, their physiological functions are not well understood. The amino acid sequences of aldose reductases and aldehyde reductases exhibit significant levels of similarity, but the amino acid sequences of carbonyl reductases do not (32).
In previous papers, we described purification and characterization of three NADPH-dependent aldehyde reductases (ARI, ARII, and ARIII) of the red yeast Sporobolomyces salmonicolor AKU4429 (9, 14, 34). ARI is the most abundant aldehyde reductase in this yeast and catalyzes asymmetric reduction of ethyl 4-chloro-3-oxobutanoate (4-COBE) to ethyl (R)-4-chloro-3-hydroxybutanoate (4-CHBE) {enantiomeric excess for (R) = [(R − S)/(R + S] × 100 and vice versa}, a promising chiral building block for organic synthesis. In contrast, ARII is produced in considerably smaller amounts but reduces 4-COBE to the (S) enantiomer (92.7% enantiomeric excess), which is also a useful chiral building block for chemical synthesis of pharmaceuticals. In addition to the stereoselectivity of activity against 4-COBE, the N-terminal amino acid sequences of these two aldehyde reductases are quite different. Based on the amino acid sequence deduced from the cDNA sequence, ARI belongs to the aldo-keto reductase superfamily (13). Recently, an NADPH-dependent aldehyde reductase (S1), which reduces 4-COBE to the (S) enantiomer (100% enantiomeric excess), was purified from Candida magnoliae AKU4643 (31). The substrate specificities, subunit structures, and N-terminal amino acid sequences of ARII and S1 are not similar. This indicates that the two enzymes belong to the different groups.
In this study, we cloned and analyzed a cDNA clone of the aldehyde reductase gene (ARII) in order to compare the catalytic mechanisms of ARI and ARII and to understand the molecular basis of the stereospecific reduction of 4-COBE.
34 citations
TL;DR: In this article, the authors present a partir essentiellement de (1,2:3,4-di-O-isopropylidene-5-[1-(trimethylsiloxy) vinyl]) arabinopyranose et de 2-acetyl 1, 4-benzoquinone.
Abstract: Synthese de (1,2:3,4-di-O-isopropylidene-5-[4,5,8-triacetoxy-2-naphtyl]) arabinopyranose a partir essentiellement de (1,2:3,4-di-O-isopropylidene-5-[1-(trimethylsiloxy) vinyl]) arabinopyranose et de 2-acetyl 1,4-benzoquinone
33 citations
TL;DR: In this article, a diastereogenic addition of 2-trimethylsilylthiazole (1) to the side-chain aldehyde and unmasking the formyl group from thiazole ring was carried out for homologation of the title dialdoses.
33 citations
TL;DR: In this paper, the 1-phenyl-3-methyl-5-pyrazolone derivatives of aldose enantiomers were well separated from each other by capillary zone electrophoresis using a neutral phosphate buffer containing an optically active N-dodecoxycarbonylvaline (DCV).
33 citations