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Literature summary for 3.2.1.23 extracted from

  • Jeong, J.K.; Kwon, O.; Lee, Y.M.; Oh, D.B.; Lee, J.M.; Kim, S.; Kim, E.H.; Le, T.N.; Rhee, D.K.; Kang, H.A.
    Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface {beta}-galactosidase with specific hydrolysis activity for the Gal{beta}1-3GlcNAc moiety of oligosaccharide (2009), J. Bacteriol., 191, 3011-3023.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
additional information the bgaC deletion mutation does not significantly attenuate the virulence of Streptococcus pneumoniae in vivo, but the bgaC mutant strain shows relatively low numbers of viable cells compared to the wild type after 24 h of infection in vivo. The mutant shows higher colonization levels at 6 and 24 h postinfection in vivo Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Streptococcus pneumoniae 9986
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Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q8DRL4 isoform BgaC
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme displays a highly regiospecific and sugar-specific hydrolysis activity for the Gal-beta(1-3)-GlcNAc moiety of oligosaccharides Streptococcus pneumoniae ?
-
 ?