EC - Endo-α-N-acetylgalactosaminidase

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IntEnz Enzyme Nomenclature


Accepted name:
Other names:
mucinaminylserine mucinaminidase
D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase
glycopeptide α-N-acetylgalactosaminidase
D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Systematic name:
glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase



The enzyme catalyses the liberation of Gal-(1→3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. release of the core 2 trisaccharide Gal-(1→3)-β-(GlcNAc-(1→6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1→3)-β-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033926 , GO:0050110
CAS Registry Number: 59793-96-3


  1. Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M., Yamamoto, K.
    Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens.
    Glycobiology 18: 727-734 (2008). [PMID: 18559962]
  2. Koutsioulis, D., Landry, D., Guthrie, E. P.
    Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity.
    Glycobiology 18: 799-805 (2008). [PMID: 18635885]
  3. Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H., Yamamoto, K.
    Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum.
    J. Biol. Chem. 280: 37415-37422 (2005). [PMID: 16141207]
  4. Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K., Fushinobu, S.
    Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum.
    J. Biochem. 146: 389-398 (2009). [PMID: 19502354]
  5. Gregg, K. J., Boraston, A. B.
    Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65: 133-135 (2009). [PMID: 19194003]
  6. Ashida, H., Yamamoto, K., Murata, T., Usui, T., Kumagai, H.
    Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity.
    Arch. Biochem. Biophys. 373: 394-400 (2000). [PMID: 10620364]
  7. Goda, H. M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H., Ito, M.
    Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis.
    Biochem. Biophys. Res. Commun. 375: 441-446 (2008). [PMID: 18725192]

[EC created 1978 (EC created 1984, incorporated 2008), modified 2008, modified 2011]