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Merck

Acceptor specificity in the transglycosylation reaction using Endo-M.

Carbohydrate research (2010-10-12)
Yusuke Tomabechi, Yuki Odate, Ryuko Izumi, Katsuji Haneda, Toshiyuki Inazu
RÉSUMÉ

To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to 6-hydroxy functions of GlcNAc were found to be essential for the transglycosylation reaction using Endo-M. Furthermore, it was determined that Endo-M strictly recognizes a 1,3-diol structure consisting of primary and secondary hydroxyl groups.

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Sigma-Aldrich
Endoglycosidase H from Streptomyces plicatus, recombinant, expressed in E. coli, buffered aqueous solution
Sigma-Aldrich
Endoglycosidase F1, recombinant, expressed in E. coli, ≥16 U/mg, buffered aqueous solution
Sigma-Aldrich
Endoglycosidase F3 from Elizabethkingia miricola, recombinant, expressed in E. coli, 30 U/mg
Sigma-Aldrich
Endoglycosidase F2 from Elizabethkingia miricola, recombinant, expressed in E. coli, 20 U/mg