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Literature summary for 3.2.1.96 extracted from

  • Yamamoto, S.; Muramatsu, H.; Muramatsu, T.
    Mutational studies on endo-beta-N-acetylglucosaminidase D which hydrolyzes core portion of asparagine-linked complex type oligosaccharides (2005), Glycoconj. J., 22, 35-42.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli TOP10, enzymes with truncation or point mutation Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
del316/delY319/E320 mutation completely removes the activity for (Man)5(GlcNAc)2Asn, a low level of activity towards (Man)3(GlcNAc)2Asn remains Streptococcus pneumoniae
delE324 loss of activity Streptococcus pneumoniae
delW359/delY360 loss of activity Streptococcus pneumoniae
additional information truncated enzyme form in which 134 N-terminal and 599-C-tterminal amino acids are deleted, still retains enzymatic activity. The specificity of the truncated enzyme is indistinguishable from the intact enzyme and also acts on the core structure of the asparagine-linked oligosaccharides attached to intact IgG Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complex-type aspargine-linked oligosaccharide + H2O hydrolysis of the di-N-acetylchitobiose structure. The specificity for complex type oligosaccharides is probably defined by multiple domains in Endo D structure Streptococcus pneumoniae ?
-
?

Synonyms

Synonyms Comment Organism
Endo D
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Streptococcus pneumoniae
endo-beta-N-acetylglucosaminidase D
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Streptococcus pneumoniae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
5 min, about 90% loss of activity Streptococcus pneumoniae
55
-
5 min, about 65% loss of activity Streptococcus pneumoniae