Microbial Glycosyltransferases for Carbohydrate Synthesis: a-2,3-Sialyltransferase from Neisseria gonorrheae

Research output: Contribution to journalArticleResearchpeer review

Authors

  • M. Izumi
  • G. J. Shen
  • S. Wacowich-Sgarbi
  • T. Nakatani
  • O. Plettenburg
  • C. H. Wong

External Research Organisations

  • The Scripps Research Translational Institute
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Details

Original languageEnglish
Pages (from-to)10909-10918
Number of pages10
JournalJournal of the American Chemical Society
Volume123
Issue number44
Early online date10 Oct 2001
Publication statusPublished - 7 Nov 2001
Externally publishedYes

Abstract

The α-2,3-sialyltransferase from Neisseria gonorrheae was overproduced in E. coli for exploitation of its substrate specificity and synthetic utility. Several potential acceptor substrates were synthesized in this study, including mono- and oligosaccharides, glycolipids, and glycopeptides and their sulfate derivatives. Some CMP-sialic acid derivatives with modification at the C-5 position were also prepared for evaluation as donor substrates. It was found that the enzyme exhibits a broader acceptor substrate specificity when compared to other sialyltransferases, though the donor specificity is quite limited. Application of the enzyme to the preparative synthesis of representative sialyl glycoconjugates has been demonstrated. On the basis of this work and the work of others, this enzyme is the most versatile and synthetically useful among all sialyltransferases known to date, especially for the synthesis of sulfate-containing glycoconjugates.

ASJC Scopus subject areas

Cite this

Microbial Glycosyltransferases for Carbohydrate Synthesis: a-2,3-Sialyltransferase from Neisseria gonorrheae. / Izumi, M.; Shen, G. J.; Wacowich-Sgarbi, S. et al.
In: Journal of the American Chemical Society, Vol. 123, No. 44, 07.11.2001, p. 10909-10918.

Research output: Contribution to journalArticleResearchpeer review

Izumi M, Shen GJ, Wacowich-Sgarbi S, Nakatani T, Plettenburg O, Wong CH. Microbial Glycosyltransferases for Carbohydrate Synthesis: a-2,3-Sialyltransferase from Neisseria gonorrheae. Journal of the American Chemical Society. 2001 Nov 7;123(44):10909-10918. Epub 2001 Oct 10. doi: 10.1021/ja011382r
Izumi, M. ; Shen, G. J. ; Wacowich-Sgarbi, S. et al. / Microbial Glycosyltransferases for Carbohydrate Synthesis : a-2,3-Sialyltransferase from Neisseria gonorrheae. In: Journal of the American Chemical Society. 2001 ; Vol. 123, No. 44. pp. 10909-10918.
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abstract = "The α-2,3-sialyltransferase from Neisseria gonorrheae was overproduced in E. coli for exploitation of its substrate specificity and synthetic utility. Several potential acceptor substrates were synthesized in this study, including mono- and oligosaccharides, glycolipids, and glycopeptides and their sulfate derivatives. Some CMP-sialic acid derivatives with modification at the C-5 position were also prepared for evaluation as donor substrates. It was found that the enzyme exhibits a broader acceptor substrate specificity when compared to other sialyltransferases, though the donor specificity is quite limited. Application of the enzyme to the preparative synthesis of representative sialyl glycoconjugates has been demonstrated. On the basis of this work and the work of others, this enzyme is the most versatile and synthetically useful among all sialyltransferases known to date, especially for the synthesis of sulfate-containing glycoconjugates.",
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T2 - a-2,3-Sialyltransferase from Neisseria gonorrheae

AU - Izumi, M.

AU - Shen, G. J.

AU - Wacowich-Sgarbi, S.

AU - Nakatani, T.

AU - Plettenburg, O.

AU - Wong, C. H.

N1 - Funding Information: This research was supported by the NIH (GM44154). Oliver Plettenburg acknowledges a fellowship of the Deutsche Forschungsgemeinschaft.

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AB - The α-2,3-sialyltransferase from Neisseria gonorrheae was overproduced in E. coli for exploitation of its substrate specificity and synthetic utility. Several potential acceptor substrates were synthesized in this study, including mono- and oligosaccharides, glycolipids, and glycopeptides and their sulfate derivatives. Some CMP-sialic acid derivatives with modification at the C-5 position were also prepared for evaluation as donor substrates. It was found that the enzyme exhibits a broader acceptor substrate specificity when compared to other sialyltransferases, though the donor specificity is quite limited. Application of the enzyme to the preparative synthesis of representative sialyl glycoconjugates has been demonstrated. On the basis of this work and the work of others, this enzyme is the most versatile and synthetically useful among all sialyltransferases known to date, especially for the synthesis of sulfate-containing glycoconjugates.

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