ReviewProtein and peptide letters2017
Glycan Phosphorylases in Multi-Enzyme Synthetic Processes.
Review in Protein and peptide letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed.
- Efficient Synthesis of β-Glucose 1-Phosphate through Enzymatic Phosphorolysis and Baker's Yeast Fermentation.Journal of applied glycoscience · 2024Article
- Small tools for sweet challenges: advances in microfluidic technologies for glycan synthesis.Analytical and bioanalytical chemistry · 2022Review
- Engineering cascade biocatalysis in whole cells for bottom-up synthesis of cello-oligosaccharides: flux control over three enzymatic steps enables soluble production.Microbial cell factories · 2022Article
- Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022Review
- Stoichiometric Conversion of Maltose for Biomanufacturing byBiodesign research · 2022Article
- Molecular Recognition of Natural and Non-Natural Substrates by Cellodextrin Phosphorylase from Ruminiclostridium Thermocellum Investigated by NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Recent advances in enzymatic synthesis of β-glucan and cellulose.Carbohydrate research · 2021Review
- Recent progress in synthesis of carbohydrates with sugar nucleotide-dependent glycosyltransferases.Current opinion in chemical biology · 2021Review
- Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution.Synthetic and systems biotechnology · 2021Article
- Chemoenzymatic Synthesis of Fluorinated Cellodextrins Identifies a New Allomorph for Cellulose-Like Materials*.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Genomic and Transcriptome Analyses of a Thermophilic BacteriumMicroorganisms · 2020Article
- Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof.Chembiochem : a European journal of chemical biology · 2020Article
- Article
- Product solubility control in cellooligosaccharide production by coupled cellobiose and cellodextrin phosphorylase.Biotechnology and bioengineering · 2019Article
- Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase families.The Journal of biological chemistry · 2019Article
- Harnessing glycoenzyme engineering for synthesis of bioactive oligosaccharides.Interface focus · 2019Review
- Identification ofThe Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glycosylation with concomitant release of inorganic phosphate. The equilibrium position of such reactions can render them of limited synthetic utility, unless coupled with a secondary enzymatic step where the reaction lies heavily in favour of product. This article surveys recent works on the combined use of glycan phosphorylases with other enzymes to achieve synthetically useful processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.