Chemoenzymatic Synthesis of Glycans and Glycoconjugates

Review
In: Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015. Chapter 54.
2017.

Excerpt

Glycosyltransferases are the biosynthetic enzymes responsible for the construction of interglycosidic linkages, and glycosidases catalyze the opposite reaction, hydrolysis of interglycosidic linkages (Chapter 6). The diversity of natural glycans is reflected by the numerous glycosyltransferases and glycosidases encountered in nature, each showing a defined substrate specificity. Natural glycans are often encountered in heterogeneous form and often produced in minute amounts, making their isolation and characterization from natural sources often cumbersome. Therefore, glycobiology relies heavily on synthetic glycans, and synthetic methodology to produce glycans has witnessed tremendous progress in the past two decades (Chapter 53). Glycosyltransferases and glycosidases offer several advantages in the construction of glycans. Especially under controlled conditions, these biocatalysts are very powerful. Here, recent developments in the use of (mutant) glycosidases and glycosyltransferases for the synthesis of tailored glycans, including combinations of both enzyme classes and in conjunction with synthetic intermediates, are presented.

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