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Synthesis of Sialyl T N Glycopeptides – Enzymatic Sialylation by α2,6‐Sialyltransferase from Photobacterium damsela
Author(s) -
Teo ChinFen,
Hwang TzannShun,
Chen PeiHeng,
Hung ChihHung,
Gao HeauShan,
Chang LeeShang,
Lin ChunHung
Publication year - 2005
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200505061
Subject(s) - chemistry , sialyltransferase , photobacterium , glycopeptide , threonine , enzyme , biochemistry , glycoconjugate , serine , residue (chemistry) , stereochemistry , moiety , bacteria , biology , vibrio , genetics , antibiotics
The α2,6‐sialyltransferase from Photobacterium damsela was applied for the enzymatic sialylation of the T N 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