Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.23 expression in Escherichia coli Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.23 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

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.23 Streptococcus pneumoniae Q8DRL4 isoform BgaC
-

Substrates and Products (Substrate)

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