Glycopeptide alpha-N-acetylgalactosaminidase

Endo-α-N-acetylgalactosaminidase
Identifiers
EC number	3.2.1.97
CAS number	59793-96-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase.^{[1][2][3][4][5][6][7]} This enzyme catalyses the following chemical reaction

3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H₂O $\rightleftharpoons$ 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein]

The enzyme catalyses the release of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins.

Glycopeptide α-N-acetylgalactosaminidases belong to family GH101 of glycoside hydrolases.^[8]

References

1. Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M. and Yamamoto, K. (2008). "Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens". Glycobiology 18 (9): 727–734. doi:10.1093/glycob/cwn053. PMID 18559962.
2. Koutsioulis, D., Landry, D. and Guthrie, E.P. (2008). "Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity". Glycobiology 18 (10): 799–805. doi:10.1093/glycob/cwn069. PMID 18635885.
3. Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H. and Yamamoto, K. (2005). "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 (45): 37415–37422. doi:10.1074/jbc.m506874200. PMID 16141207.
4. Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K. and Fushinobu, S. (2009). "Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum". J. Biochem. 146 (3): 389–398. doi:10.1093/jb/mvp086. PMID 19502354.
5. Gregg, K.J. and Boraston, A.B. (2009). "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 (Pt 2): 133–135. doi:10.1107/s1744309108042474. PMID 19194003.
6. Ashida, H., Yamamoto, K., Murata, T., Usui, T. and Kumagai, H. (2000). "Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity". Arch. Biochem. Biophys. 373 (2): 394–400. doi:10.1006/abbi.1999.1565. PMID 10620364.
7. Goda, H.M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H. and Ito, M. (2008). "Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis". Biochem. Biophys. Res. Commun. 375 (4): 441–446. doi:10.1016/j.bbrc.2008.08.065. PMID 18725192.
8. Naumoff DG (2010). "GH101 family of glycoside hydrolases: subfamily structure and evolutionary connections with other families.". J Bioinform Comput Biol 8 (3): 437–451. doi:10.1142/s0219720010004628. PMID 20556855.

External links

• Endo-alpha-N-acetylgalactosaminidase at the US National Library of Medicine Medical Subject Headings (MeSH)