ArticleAnalytical biochemistry2008
A comparison of sugar indicators enables a universal high-throughput sugar-1-phosphate nucleotidyltransferase assay.
Article in Analytical biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 69 citations in OpenAlex.
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- Glucose Uptake and Oxidative Stress in Caco-2 Cells: Health Benefits fromMarine drugs · 2022Article
- Carbohydrate Metabolism in Bacteria: Alternative Specificities in ADP-Glucose Pyrophosphorylases Open Novel Metabolic Scenarios and Biotechnological Tools.Frontiers in microbiology · 2022Article
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- Investigating the structural properties and in vitro digestion of rice flours.Food science & nutrition · 2021Article
- Use of Amylomaltase to Steer the Functional and Nutritional Properties of Wheat Starch.Foods (Basel, Switzerland) · 2021Article
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- The single berberine bridge enzyme homolog of Physcomitrella patens is a cellobiose oxidase.The FEBS journal · 2018Article
- Accurate Quantification of Laminarin in Marine Organic Matter with Enzymes from Marine Microbes.Applied and environmental microbiology · 2017Article
- Cellulolytic RoboLector - towards an automated high-throughput screening platform for recombinant cellulase expression.Journal of biological engineering · 2017Article
- Expanding the nucleotide and sugar 1-phosphate promiscuity of nucleotidyltransferase RmlA via directed evolution.The Journal of biological chemistry · 2011Article
- The in vitro characterization of polyene glycosyltransferases AmphDI and NysDI.Chembiochem : a European journal of chemical biology · 2008Article
- The impact of enzyme engineering upon natural product glycodiversification.Current opinion in chemical biology · 2008Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A systematic comparison of six sugar indicators for their sensitivity, specificity, cross-reactivity, and suitability in the context of crude lysates revealed para-hydroxybenzoic acid hydrazide (pHBH) to be best suited for application in a plate-based phosphatase-assisted universal sugar-1-phosphate nucleotidyltransferase assay. The addition of a general phosphatase to nucleotidyltransferase reaction aliquots enabled the conversion of remaining sugar-1-phosphate to free sugar, the concentration of which could be rapidly assessed via the pHBH assay. The assay was validated using the model glucose-1-phosphate thymidylyltransferase from Salmonella enterica (RmlA) and compared favorably with a previously reported HPLC assay. This coupled discontinuous assay is quantitative, high throughput, and robust; relies only on commercially available enzymes and reagents; does not require chromatography, specialized detectors (e.g., mass or evaporative light scattering detectors), or radioisotopes; and is capable of detecting less than 5 nmol of sugar-1-phosphate. It is anticipated that this high-throughput assay system will greatly facilitate nucleotidyltransferase mechanistic and directed evolution/engineering studies.
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Registered trials
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