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.
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12 citations
12 citations
TL;DR: Novel crystal structures of the dimeric Cc AAOR in complex with the cofactor and glycerol, D-xylose,D-glucose, maltotriose and D-sorbitol allowed for a detailed analysis of the ligand-binding interactions and showed that the C1 carbon of a substrate is close to the reactive C4 carbon of the nicotinamide ring of NADP(H).
Abstract: Aldose–aldose oxidoreductase ( Cc AAOR) is a recently characterized enzyme from the bacterial strain Caulobacter crescentus CB15 belonging to the glucose-fructose oxidoreductase/inositol dehydrogenase/rhizopine catabolism protein (Gfo/Idh/MocA) family. Cc AAOR catalyses the oxidation and reduction of a panel of aldose monosaccharides using a tightly bound NADP(H) cofactor that is regenerated in the catalytic cycle. Furthermore, Cc AAOR can also oxidize 1,4-linked oligosaccharides. In the present study, we present novel crystal structures of the dimeric Cc AAOR in complex with the cofactor and glycerol, D-xylose, D-glucose, maltotriose and D-sorbitol determined to resolutions of 2.0, 1.8, 1.7, 1.9 and 1.8 A (1 A=0.1 nm), respectively. These complex structures allowed for a detailed analysis of the ligand-binding interactions. The structures showed that the C1 carbon of a substrate, which is either reduced or oxidized, is close to the reactive C4 carbon of the nicotinamide ring of NADP(H). In addition, the O1 hydroxy group of the substrate, which is either protonated or deprotonated, is unexpectedly close to both Lys104 and Tyr189, which may both act as a proton donor or acceptor. This led us to hypothesize that this intriguing feature could be beneficial for Cc AAOR to catalyse the reduction of a linear form of a monosaccharide substrate and the oxidation of a pyranose form of the same substrate in a reaction cycle, during which the bound cofactor is regenerated.
* Cc AAOR, : Caulobacter crescentus aldose–aldose oxidoreductase; PDB, : Protein Data bank; Zm GFOR, : Zymomonas mobilis glucose–fructose oxidoreductase
12 citations
TL;DR: In this article, treatment of unprotected methyl-α-D-glucopyranoside, N-acetylglucosamine and maltose with triphenylphosphine, diethylazodicarboxylate and equimolar amount of various carboxylic acids allowed regioselective 6-O-esterifications (6′-O for maltose) of the carbohydrate without esterification of other hydroxyl groups.
12 citations
Patent•
29 Oct 1991
TL;DR: In this paper, a method for quantitative determination of aldoses, in particular xylose, was presented. But this method was not applicable to the determination of monomeric aldose units of oligomeric sugars.
Abstract: The present invention relates to a method for quantitative determination of aldoses, in particular xylose. According to the method, the aldose is enzymatically oxidized to the corresponding aldonolactone with the aid of an aldose dehydrogenase in the presence of an electron acceptor. The amount of the reduced electron acceptor is determined as a measure of the amount aldose. According to the invention, a PQQ-linked aldose dehydrogenase enzyme is used for oxidizing the aldose. The enzyme is preferably obtained from strains of the genus Gluconobacter. The invention also concerns a method for determining the monomeric aldose units of oligomeric sugars. By immobilizing the aldose dehydrogenase enzyme on an electrode, a aldose biosensor is provided which can be used for electrochemical methods for determination of aldoses.
12 citations