Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Pergolizzi, Giulia, Kuhaudomlarp, Sakonwan, Kalita, Eeshan, Field, Robert A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Science Publishers 2017
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
_version_ 1783279162813841408
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
work_keys_str_mv AT pergolizzigiulia glycanphosphorylasesinmultienzymesyntheticprocesses
AT kuhaudomlarpsakonwan glycanphosphorylasesinmultienzymesyntheticprocesses
AT kalitaeeshan glycanphosphorylasesinmultienzymesyntheticprocesses
AT fieldroberta glycanphosphorylasesinmultienzymesyntheticprocesses