Synthesis of Sialyl TN Glycopeptides - Enzymatic Sialylation by α2,6-Sialyltransferase from Photobacterium damsela

The α2,6‐sialyltransferase from Photobacterium damsela was applied for the enzymatic sialylation of the TN glycopeptide (APGSTA) with GalNAc α‐linked to either the serine or threonine residue in the sequence. The enzyme preparation and reaction conditions were optimized prior to the application. In...

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Bibliographic Details
Published in:Advanced synthesis & catalysis 2005-06, Vol.347 (7-8), p.967-972
Main Authors: Teo, Chin-Fen, Hwang, Tzann-Shun, Chen, Pei-Heng, Hung, Chih-Hung, Gao, Heau-Shan, Chang, Lee-Shang, Lin, Chun-Hung
Format: Article
Language:English
Subjects:
antigens
enzyme catalysis
glycopeptides
glycosylation
sialic acids
Online Access:Get full text
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Summary:The α2,6‐sialyltransferase from Photobacterium damsela was applied for the enzymatic sialylation of the TN glycopeptide (APGSTA) with GalNAc α‐linked to either the serine or threonine residue in the sequence. The enzyme preparation and reaction conditions were optimized prior to the application. In contrast to the mammalian sialyltransferases which recognize the moiety of GalNAcα(1,1)Thr only, this bacterial enzyme can accept GalNAcα(1,1)Thr as well as GalNAcα(1,1)Ser. Our study also introduced a 4‐dimethylaminoazobenzene‐4′‐sulfonyl (dabsyl) chromophore to the N‐terminus of the peptide backbone, which is suitable for glycoconjugate substrates without affecting the binding affinity
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.200505061