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Glycoside phosphorylases: Structure, catalytic properties and biotechnological potential ☆

Paper ID Volume ID Publish Year Pages File Format Full-Text
14212 1189 2015 16 PDF Available
Title
Glycoside phosphorylases: Structure, catalytic properties and biotechnological potential ☆
Abstract

Glycoside phosphorylases (GPs) are the enzymes that reversibly phosphorolytically process glycosidic bond in sucrose (6′-phosphate), α-1,4-glucan and maltodextrins, α-glucobioses, α-1,3-oligoglucan, β-glucobioses and β-glucodextrins, chitobiose, β-galactosides and β-mannosides, and transfer non-reducing end terminal glycosyl residue to inorganic phosphate. They are modular enzymes that form biologically active homooligomers. From a mechanistic as well as structural point of view, they are similar to glycoside hydrolases or glycosyltransferases. Regardless the stereochemical outcome of the phosphorylase-catalyzed reaction (inversion or retention) the phosphorolytic cleavage of glycosidic bond is reversible, therefore glycosyl phosphates may efficiently be used for oligosaccharide synthesis. Although majority of GPs show very high substrate and positional selectivity, they might be employed for a green, inexpensive and often one-pot conversion of one sugar (cheap) to another one (expensive). This fascinating capability is due to the fact that pathways of several GPs share the same glycosyl phosphate, i.e. a product of one phosphorylase is simultaneously consumed as a substrate by another one, or even the same enzyme in a second step if the phosphorylase possesses a relaxed acceptor specificity. In some cases glycosyl phosphates may be interconverted using other auxiliary carbohydrate-active enzymes, achieving for example galactoside synthesis from gluco-configured sugar donors, thus widening synthetic potential of these biocatalysts. In comparison with common hydrolysis, the energy of glycosidic bond is not annihilated during phosphorolysis. This energetic aspect of the reactions catalyzed by GPs and their physiological role is discussed in relation to often concurrently occurring glycoside hydrolases.

Keywords
GH, glycoside hydrolase; GP, glycoside phosphorylase; GT, glycosyltransferaseGlycosidic bond; Phosphorolysis; Glycoside phosphorylase; Oligosaccharide synthesis
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Glycoside phosphorylases: Structure, catalytic properties and biotechnological potential ☆
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biotechnology Advances - Volume 33, Issue 2, March–April 2015, Pages 261–276
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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