Glycan phosphorylases in multi-enzyme synthetic processes

Pergolizzi, Giulia, Kuhaudomlarp, Sakonwan, Kalita, Eeshan and Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 (2017) Glycan phosphorylases in multi-enzyme synthetic processes. Protein and Peptide Letters, 24 (8). pp. 696-709. ISSN 0929-8665

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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.

Item Type:	Article
Additional Information:	Funding Information: These studies were supported by the UK BBSRC Institute Strategic Program on Understanding and Exploiting Metabolism (MET) BB/J[004561/1] nd ahe JthnoInens Foundation; BBSRC, EPSRC and InnovateUK: IBCatalyst [BB/M02903411]; Royal Thai Government Scholarship; DBT Overseas Associateship (NER), Govt. of India, [BT/20/NE/2011]. Publisher Copyright: © 2017 Bentham Science Publishers.
Uncontrolled Keywords:	biofuel.,cellodextrin,disaccharide,high-value products,phosphorylase,α-glucan,structural biology,biochemistry ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	04 Sep 2024 09:35
Last Modified:	25 Sep 2024 18:06
URI:	https://ueaeprints.uea.ac.uk/id/eprint/96510
DOI:	10.2174/0929866524666170811125109

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