Glycan phosphorylases in multi-enzyme synthetic processes

G. Pergolizzi; S. Kuhaudomlarp; E. Kalita; R.A. Field

doi:10.2174/0929866524666170811125109

Glycan phosphorylases in multi-enzyme synthetic processes

G. Pergolizzi, S. Kuhaudomlarp, E. Kalita, R.A. Field

Manchester Institute of Biotechnology

Research output: Contribution to journal › Review article › peer-review

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.

Original language	English
Journal	Protein and Peptide Letters
DOIs	https://doi.org/10.2174/0929866524666170811125109
Publication status	Published - 24 Jun 2017

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Manchester Institute of Biotechnology

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10.2174/0929866524666170811125109

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title = "Glycan phosphorylases in multi-enzyme synthetic processes",

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.",

author = "G. Pergolizzi and S. Kuhaudomlarp and E. Kalita and R.A. Field",

year = "2017",

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T1 - Glycan phosphorylases in multi-enzyme synthetic processes

AU - Pergolizzi, G.

AU - Kuhaudomlarp, S.

AU - Kalita, E.

AU - Field, R.A.

PY - 2017/6/24

Y1 - 2017/6/24

N2 - 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.

AB - 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.

U2 - 10.2174/0929866524666170811125109

DO - 10.2174/0929866524666170811125109

M3 - Review article

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

ER -

Glycan phosphorylases in multi-enzyme synthetic processes

Abstract

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UN SDGs

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