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Literature summary for 3.2.1.97 extracted from

  • Ashida, H.; Ozawa, H.; Fujita, K.; Suzuki, S.; Yamamoto, K.
    Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-alpha-N-acetylgalactosaminidase (2010), Glycoconj. J., 27, 125-132.
    View publication on PubMed
Search for more literature for 3.2.1.97

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged EngBF in Escherichia coli strain BL21(DE3) Bifidobacterium longum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bifidobacterium longum EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides ?
-
 ?
additional information Bifidobacterium longum JCM 1217 EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bifidobacterium longum
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 strain JCM1217, ATCC29521
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Bifidobacterium longum JCM 1217
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 strain JCM1217, ATCC29521
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged EngBF from Escherichia coli strain BL21(DE3) by affinity chromatography and gel filtration Bifidobacterium longum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
-
 Bifidobacterium longum 4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
 ?
4-nitrophenyl beta-D-Gal-(1->3)-alpha-D-GalNAc + H2O
-
 Bifidobacterium longum JCM 1217 4-nitrophenol + beta-D-Gal-(1->3)-alpha-D-GalNAc
-
 ?
additional information EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides Bifidobacterium longum ?
-
 ?
additional information endo-alpha-N-acetylgalactosaminidase catalyzes the release of Galbeta1-3GalNAc from the core 1-type O-glycan, Galbeta1-3GalNAcalpha1-Ser/Thr, of mucin glycoproteins and synthetic 4-nitrophenyl alpha-linked substrates. The enzyme directly transfers Galbeta1-3GalNAc to serine or threonine residues of bioactive peptides such as PAMP-12, bradykinin, peptide-TandMUC1a when Galbeta1-3GalNAcalpha1-4NP was used as a donor substrate. The enzyme also catalyzes the reverse-hydrolysis reaction. EngBF synthesizes the core 1 disaccharide-containing oligosaccharides when the enzyme is incubated with either glucose or lactose and Galbeta1-3GalNAc Bifidobacterium longum ?
-
 ?
additional information EngBF preferably releases Galbeta1-3GalNAc from the core 1-type O-glycan, i.e. Thomsen-Friedenreich antigen or T-antigen, of mucin glycoproteins. EngBF also shows transglycosylation activity of the released disaccharide to other mono- and disaccharides Bifidobacterium longum JCM 1217 ?
-
 ?
additional information endo-alpha-N-acetylgalactosaminidase catalyzes the release of Galbeta1-3GalNAc from the core 1-type O-glycan, Galbeta1-3GalNAcalpha1-Ser/Thr, of mucin glycoproteins and synthetic 4-nitrophenyl alpha-linked substrates. The enzyme directly transfers Galbeta1-3GalNAc to serine or threonine residues of bioactive peptides such as PAMP-12, bradykinin, peptide-TandMUC1a when Galbeta1-3GalNAcalpha1-4NP was used as a donor substrate. The enzyme also catalyzes the reverse-hydrolysis reaction. EngBF synthesizes the core 1 disaccharide-containing oligosaccharides when the enzyme is incubated with either glucose or lactose and Galbeta1-3GalNAc Bifidobacterium longum JCM 1217 ?
-
 ?

Synonyms

Synonyms Comment Organism
endo-alpha-N-acetylgalactosaminidase
-
 Bifidobacterium longum
EngBF
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 Bifidobacterium longum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bifidobacterium longum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Bifidobacterium longum