General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability.
General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability.
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DOI:
10.1002/anie.202112574
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发表时间:
2021-12-13
期刊:
影响因子:
--
通讯作者:
Li L
中科院分区:
文献类型:
--
作者:
Fu X;Gadi MR;Wang S;Han J;Liu D;Chen X;Yin J;Li L
Accessing large numbers of structurally diverse glycans and derivatives is essential to functional glycomics. We showed a general tolerance of galactosyltransferases toward uridine-diphosphate-galactosamine (UDP-GalN), which is not a commonly used sugar nucleotide donor. The property was harnessed to develop a two-step chemoenzymatic strategy for facile synthesis of novel and divergent N-acetylgalactosamine (GalNAc)-glycosides and derivatives in preparative scales. The discovery and the application of the new property of existing glycosyltransferases expand their catalytic capabilities in generating novel carbohydrate linkages, thus prompting the synthesis of diverse glycans and glycoconjugates for biological studies. Preparation of diverse glycans is essential to glycobiology, while synthetic-useful enzymes for this purpose are limited. This study discovered a general tolerance of galactosyltransferases (GalTs) toward uncommon donor UDP-galactosamine. A two-step strategy was devised to harness this property for the facile synthesis of GalNAc-glycosides. The newly identified catalytic properties of GalTs would greatly expand their utilization in chemical glycobiology.
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影响因子:
4.4
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DOI:
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发表时间:
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影响因子:
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