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Literature summary for 3.2.1.96 extracted from

  • Ochiai, H.; Huang, W.; Wang, L.X.
    Endo-beta-N-acetylglucosaminidase-catalyzed polymerization of beta-Glcp-(1-->4)-GlcpNAc oxazoline: a revisit to enzymatic transglycosylation (2009), Carbohydr. Res., 344, 592-598.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
additional information polymerization by endo-beta-N-acetylglucosaminidase may find useful applications for the synthesis of novel artificial polysaccharides Glutamicibacter protophormiae

Cloned(Commentary)

Cloned (Comment) Organism
pGEX-2T/Endo-A plasmid overexpressed in Escherichia coli Glutamicibacter protophormiae

Organism

Organism UniProt Comment Textmining
Glutamicibacter protophormiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-Glcp-(1-4)-GlcpNAc-oxazoline Endo-A shows only marginal activity for transglycosylation with the disaccharide oxazoline. When used in a relatively large quantity, Endo-A can promote the transglycosylation of the disaccharide oxazoline to a GlcpNAc-Asn acceptor (it catalyzes the transfer of alpha-Manp-(1-3)-beta-Glcp-(1-4)-GlcpNAc-oxazoline to the acceptor). Endo-A promotes polymerization of beta-Glcp-(1-4)-GlcpNAc-oxazoline Glutamicibacter protophormiae ?
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Synonyms

Synonyms Comment Organism
Endo-A
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Glutamicibacter protophormiae
endo-beta-N-acetylglucosaminidase
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Glutamicibacter protophormiae