Exo- and endoglycosidases revisited

Many glycosidases, which work as useful reagents for the studies of structures and functions of free and conjugated oligosaccharides, have been found and thoroughly purified. These enzymes are classified into exo- and endoglycosidases by their glycon specificities. Their usefulness and limits as rea...

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Bibliographic Details
Published in:Proceedings of the Japan Academy, Series B Series B, 2013/03/11, Vol.89(3), pp.97-117
Main Author: KOBATA, Akira
Format: Article
Language:English
Subjects:
aglycon specificity
Animals
Bacteria - enzymology
Bifidus factor
Carbohydrates - chemistry
Enzymes
glycon specificity
glycosidase-deficiencies
Glycoside Hydrolases - metabolism
GNB/LNB pathway
human milk oligosaccharides
Humans
Intestines - microbiology
Milk - chemistry
Physiological psychology
Review
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Summary:Many glycosidases, which work as useful reagents for the studies of structures and functions of free and conjugated oligosaccharides, have been found and thoroughly purified. These enzymes are classified into exo- and endoglycosidases by their glycon specificities. Their usefulness and limits as reagents are explained in detail in this review. Endoglycosidases, which were originally found in the culture fluid of bacteria and in the extracts of plants, are now widely found in the mammals including humans. The physiological roles of these enzymes are discussed in relation to the oligosaccharides accumulated in the urine of patients with exoglycosidase deficiencies. Furthermore, PNGase is found to play important roles in the ER-associated degradation pathway of glycoproteins. Recent studies of the glycosidases in Bifidobacteria have revealed that GNB/LNB pathway, which uniquely exist in this bacteria, works for the expression of Bifidus factor activity of human milk oligosaccharides, an important topic in the baby nutrition. This interesting field will be introduced in detail in one section of this article. (Communicated by Kunihiko SUZUKI, M.J.A.)
ISSN:0386-2208
1349-2896
DOI:10.2183/pjab.89.97