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Aldose

About: Aldose is a(n) research topic. Over the lifetime, 1270 publication(s) have been published within this topic receiving 27197 citation(s). The topic is also known as: aldoses.

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Journal ArticleDOI
Takashi Tanaka1, Tatsuya Nakashima1, Toshihisa Ueda2, Kenji Tomii1  +1 moreInstitutions (2)
TL;DR: The reaction was applied to the determination of absolute configuration the sugar residues of an aroma precursor and direct HPLC analysis of the reaction mixture and UV detection at 250 nm discriminated D- and L-enantiomers of aldoses.

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Abstract: One-pot reactions of aldoses with L-cysteine methyl ester and o-tolyl isothiocyanate yielded methyl 2-(polyhydroxyalkyl)-3-(o-tolylthiocarbamoyl)-thiazolidine-4(R)-carboxylates. Direct HPLC analysis of the reaction mixture and UV detection at 250 nm discriminated D- and L-enantiomers of aldoses. The reaction was applied to the determination of absolute configuration the sugar residues of an aroma precursor.

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595 citations


Journal ArticleDOI
Abstract: Pairs of enantiomers of nine aldoses were separated by gas-liquid chromatography on an OV-17 capillary column as the trimethylsilyl ethers of methyl 2- (polyhydroxyalkyl) -thiazolidine-4 (R) -carboxylates, which were obtained by the reaction of aldoses with L-cysteine methyl ester. This method was applied to the determination of the absolute configurations of the component monosaccharides of a Thladiantha saponin.

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522 citations


Journal ArticleDOI
TL;DR: Southern hybridization analysis of human genomic DNA indicates a multigene system for aldose reductase, suggesting the existence of additional proteins, and the aldo-keto reductases superfamily of proteins may have a more significant and hitherto not fully appreciated role in general cellular metabolism.

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Abstract: Aldehyde reductase [EC 1.1.1.2] and aldose reductase [EC 1.1.1.21] are monomeric NADPH-dependent oxidoreductases having wide substrate specificities for carbonyl compounds. These enzymes are implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. Enzyme inhibition as a direct pharmacokinetic approach to the prevention of diabetic complications resulting from the hyperglycemia of diabetes has not been effective because of nonspecificity of the inhibitors and some appreciable side effects. To understand the structural and evolutionary relationship of these enzymes, we cloned and sequenced cDNAs coding for aldose and aldehyde reductases from human liver and placental cDNA libraries. Human placental aldose reductase (open reading frame of 316 amino acids) has a 65% identity (identical plus conservative substitutions) to human liver and placental aldehyde reductase (open reading frame of 325 amino acids). The two sequences have significant identity to 2,5-diketogluconic acid reductase from corynebacterium, frog ρ-crystallin, and bovine lung prostaglandin F synthase (reductase). Southern hybridization analysis of human genomic DNA indicates a multigene system for aldose reductase, suggesting the existence of additional proteins. Thus, the aldo-keto reductase superfamily of proteins may have a more significant and hitherto not fully appreciated role in general cellular metabolism.

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425 citations


Book ChapterDOI
John E. Hodge1Institutions (1)
TL;DR: This chapter discusses the reaction that is the isomerization of an aldosylamine to a 1-amino-1-deoxy-2-ketose configuration, named after Amadori by Kuhn and Weygand, for this rearrangement was the first to demonstrate that condensation of D-glucose with an aromatic amine would yield, according to experimental conditions, two structurally different isomers.

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Abstract: Publisher Summary This chapter discusses the reaction that is the isomerization of an aldosylamine to a 1-amino-1-deoxy-2-ketose. This rearrangement was named after Amadori by Kuhn and Weygand, for Amadori was the first to demonstrate that condensation of D-glucose with an aromatic amine ( p -phenetidine, p -anisidine, or p -toluidine) would yield, according to experimental conditions, two structurally different isomers, which are not members of an α, β anomeric pair. Amadori did not realize that an isomerization (“rearrangement”) from an aldose to a ketose configuration had occurred. However, he did discern (by change of optical rotation in acid solution) that one isomer is much more labile than the other toward hydrolysis and more susceptible to decomposition on standing in the solid state in air. He recognized correctly that the labile isomer is the N -substituted glucosylamine, but he mistakenly thought that the stable isomer was a compound of the Schiff-base type. Authentic crystalline products of the Amadori rearrangement have so far been obtained only from D-glucose, D-mannose, and 5- O -trityl-D-xylose as the sugar components. Occurrence of the rearrangement (or at least 1, 2-enolization of the N -substituted glycosylamine) was demonstrated indirectly, however, by isolation and characterization of crystalline epimeric hydrogenation products derived from D- and L-arabinose and also from D-xylose.

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295 citations


Journal ArticleDOI
TL;DR: Xylose reductase from the xylose-fermenting yeast Pichia stipitis was purified to electrophoretic and spectral homogeneity via ion-exchange, affinity and high-performance gel chromatography and is an aldose reducase (EC 1.1.21).

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Abstract: Xylose reductase from the xylose-fermenting yeast Pichia stipitis was purified to electrophoretic and spectral homogeneity via ion-exchange, affinity and high-performance gel chromatography. The enzyme was active with various aldose substrates, such as DL-glyceraldehyde, L-arabinose, D-xylose, D-ribose, D-galactose and D-glucose. Hence the xylose reductase of Pichia stipitis is an aldose reductase (EC 1.1.1.21). Unlike all aldose reductases characterized so far, the enzyme from this yeast was active with both NADPH and NADH as coenzyme. The activity with NADH was approx. 70% of that with NADPH for the various aldose substrates. NADP+ was a potent inhibitor of both the NADPH- and NADH-linked xylose reduction, whereas NAD+ showed strong inhibition only with the NADH-linked reaction. These results are discussed in the context of the possible use of Pichia stipitis and similar yeasts for the anaerobic conversion of xylose into ethanol.

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284 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20221
20213
20207
20196
201813
20176

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Topic's top 5 most impactful authors

Wiesław Szeja

8 papers, 189 citations

Masanobu Hidai

8 papers, 67 citations

Shuichi Osanai

7 papers, 86 citations

Manuel Martín-Lomas

6 papers, 76 citations

Teruaki Mukaiyama

6 papers, 89 citations