Topic
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.
Papers published on a yearly basis
Papers
More filters
TL;DR: An open reading frame in the human genome (BC014916) which has high sequence similarity to previously identified bacterial aldose 1‐epimerases is identified and this sequence was cloned into a bacterial expression vector, and expressed and purified from this source.
48 citations
48 citations
TL;DR: Comparing the structure of the Leu300Pro mutant of human aldose reductase (ALR2) in complex with the inhibitor fidarestat with that of the h ALR2−fidarestat complex indicates that the hydrogen bond between theLeu300 amino group of the wild-type and the exocyclic amide Group of the inhibitor is the key determinant for the specificity of fidarest at for ALR 2 over ALR1.
Abstract: Structure of the Leu300Pro mutant of human aldose reductase (ALR2) in complex with the inhibitor fidarestat is determined. Comparison with the hALR2−fidarestat complex and the porcine aldehyde reductase (ALR1)−fidarestat complex indicates that the hydrogen bond between the Leu300 amino group of the wild-type and the exocyclic amide group of the inhibitor is the key determinant for the specificity of fidarestat for ALR2 over ALR1. Thermodynamic data also suggest an enthalpic contribution as the predominant difference in the binding energy between the aldose reductase mutant and the wild-type. An additional selectivity-determining feature is the difference in the interaction between the inhibitor and the side chain of Trp219, ordered in the present structure but disordered (corresponding Trp220) in the ALR1−fidarestat complex. Thus, the hydrogen bond (∼7 kJ/mol) corresponds to a 23-fold difference in inhibitor potency while the differences in the interactions between Trp219(ALR2) and fidarestat and between ...
48 citations
48 citations
TL;DR: In an entirely enzymatic variation of this process, soluble pyranose 2-oxidase from Trametes multicolor was employed and could be efficiently stabilized under operational conditions by the addition of bovine serum albumin together with catalase which decomposes hydrogen peroxide formed as a by-product.
Abstract: In the Cetus process crystalline D-fructose is produced from D-glucose via the intermediate 2-keto-D-glucose. Whereas the first step in the traditional process is catalyzed by the immobilized enzyme pyranose 2-oxidase, the ensuing reduction is performed by catalytic hydrogenation. In an entirely enzymatic variation of this process, soluble pyranose 2-oxidase from Trametes multicolor was employed. This biocatalyst could be efficiently stabilized under operational conditions by the addition of bovine serum albumin (BSA) together with catalase which decomposes hydrogen peroxide formed as a by-product. D-Glucose could be converted into 2-keto-D-glucose in yields above 98%. When the biocatalyst together with both stabilizing agents was separated from the product solution by ultrafiltration, it could be reutilized for several subsequent batch operation cycles. 2-Keto-D-glucose thus obtained was quantitatively reduced to D-fructose by NAD(P)-dependent aldose reductase from Candida tenuis. Two different enzymatic...
47 citations