Glycopeptide alpha-N-acetylgalactosaminidase
| Endo-α-N-acetylgalactosaminidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.97 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 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
- ^ Ashida, H.; Maki, R.; Ozawa, H.; Tani, Y.; Kiyohara, M.; Fujita, M.; Imamura, A.; Ishida, H.; Kiso, M.; 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.
- ^ Koutsioulis, D.; Landry, D.; 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.
- ^ Fujita, K.; Oura, F.; Nagamine, N.; Katayama, T.; Hiratake, J.; Sakata, K.; Kumagai, H.; 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.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Suzuki, R.; Katayama, T.; Kitaoka, M.; Kumagai, H.; Wakagi, T.; Shoun, H.; Ashida, H.; Yamamoto, K.; 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.
- ^ Gregg, K.J.; 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.
- ^ Ashida, H.; Yamamoto, K.; Murata, T.; Usui, T.; 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.
- ^ Goda, H.M.; Ushigusa, K.; Ito, H.; Okino, N.; Narimatsu, H.; 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.
- ^ Naumoff DG; evolutionary connections with other families. (2010). "GH101 family of glycoside hydrolases: subfamily structure". J Bioinform Comput Biol. 8 (3): 437–451. doi:10.1142/s0219720010004628. PMID 20556855.
External links
- Endo-alpha-N-acetylgalactosaminidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)