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Glycan Phosphorylases in Multi-Enzyme Synthetic Processes
Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glyco-sylation 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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Bentham Science Publishers
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5688430/ https://www.ncbi.nlm.nih.gov/pubmed/28799504 http://dx.doi.org/10.2174/0929866524666170811125109 |
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author | Pergolizzi, Giulia Kuhaudomlarp, Sakonwan Kalita, Eeshan Field, Robert A. |
author_facet | Pergolizzi, Giulia Kuhaudomlarp, Sakonwan Kalita, Eeshan Field, Robert A. |
author_sort | Pergolizzi, Giulia |
collection | PubMed |
description | Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glyco-sylation 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. |
format | Online Article Text |
id | pubmed-5688430 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Bentham Science Publishers |
record_format | MEDLINE/PubMed |
spelling | pubmed-56884302017-12-04 Glycan Phosphorylases in Multi-Enzyme Synthetic Processes Pergolizzi, Giulia Kuhaudomlarp, Sakonwan Kalita, Eeshan Field, Robert A. Protein Pept Lett Article Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glyco-sylation 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. Bentham Science Publishers 2017-08 2017-08 /pmc/articles/PMC5688430/ /pubmed/28799504 http://dx.doi.org/10.2174/0929866524666170811125109 Text en © 2017 Bentham Science Publishers https://creativecommons.org/licenses/by-nc/4.0/legalcode This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited. |
spellingShingle | Article Pergolizzi, Giulia Kuhaudomlarp, Sakonwan Kalita, Eeshan Field, Robert A. Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title | Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title_full | Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title_fullStr | Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title_full_unstemmed | Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title_short | Glycan Phosphorylases in Multi-Enzyme Synthetic Processes |
title_sort | glycan phosphorylases in multi-enzyme synthetic processes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5688430/ https://www.ncbi.nlm.nih.gov/pubmed/28799504 http://dx.doi.org/10.2174/0929866524666170811125109 |
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