The Amazing Transglycosylation Activity of Endo-.BETA.-N-Acetylglucosaminidases

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  • Wang Lai-Xi
    Institute of Human Virology and Department of Biochemistry & Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA

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Other Title
  • Endo-β-<I>N-</I>-Acetylglucosaminidase の驚異的糖転移能力
  • Endo-β-N-Acetylglucosaminidaseの驚異的糖転移能力[含 英語文]
  • Endo ベータ N Acetylglucosaminidase ノ キョウイテキ トウ テンイ ノウリョク ガン エイゴブン
  • The Amazing Transglycosylation Activity of Endo-β-N-Acetylglucosaminidases
  • The amazing transglycosylation activity of endo-β-<italic>N</italic>-acetylglucosaminidases

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Abstract

Major advances have been made in exploring the trans-glycosylation activity of endo-β-N--acetylglucosaminidases (ENGases) for synthetic purpose. The exploration of synthetic sugar oxazolines as donor substrates for the ENGase-catalyzed transglycosylation has expanded the substrate availability and significantly enhanced the overall transglycosylation efficiency. On the other hand, site-directed mutagenesis in combination with activity screening has led to the discovery of the first generation ENGase-based glycosynthases that can use highly active sugar oxazolines as substrates for transglycosylation but lack hydrolytic activity on the ground-state products. ENGases have shown amazing flexibility in transglycosylation and possess much broader substrate specificity than previously thought. Now the ENGase-based chemoenzymatic method has been extended to the synthesis of a range of complex carbohydrates, including homogeneous glycopeptides, glycoproteins carrying well-defined glycans, novel oligosaccharide clusters, unusually glycosylated natural products, and even polysaccharides. This article highlights recent advances related to ENGase-catalyzed transglycosylation with a focus on their synthetic potential.

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