Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 10909-10918 |
| Seitenumfang | 10 |
| Fachzeitschrift | Journal of the American Chemical Society |
| Jahrgang | 123 |
| Ausgabenummer | 44 |
| Frühes Online-Datum | 10 Okt. 2001 |
| Publikationsstatus | Veröffentlicht - 7 Nov. 2001 |
| Extern publiziert | Ja |
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 Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemie (insg.)
- Allgemeine Chemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Chemische Verfahrenstechnik (insg.)
- Kolloid- und Oberflächenchemie
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in: Journal of the American Chemical Society, Jahrgang 123, Nr. 44, 07.11.2001, S. 10909-10918.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Microbial Glycosyltransferases for Carbohydrate Synthesis
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.
PY - 2001/11/7
Y1 - 2001/11/7
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0035823813&partnerID=8YFLogxK
U2 - 10.1021/ja011382r
DO - 10.1021/ja011382r
M3 - Article
C2 - 11686694
AN - SCOPUS:0035823813
VL - 123
SP - 10909
EP - 10918
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 44
ER -