| EC |
3.2.1.97 |
| Accepted name: |
glycopeptide α-N-acetylgalactosaminidase |
| Reaction: |
Hydrolysis of O-glycosidic linkages of sugar chains between α-N-acetyl-D-galactosamine and serine or threonine residues in glycoproteins |
| Other name(s): |
endo-α-N-acetylgalactosaminidase; 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 |
| Systematic name: |
D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase |
| Comments: |
The inability of the enzyme to hydrolyse substrates such as NeuAc→Gal→GalNAc-Ser/Thr, GalNAc→Gal→GalNAc→Ser/Thr, GalNAc→(Fuc)→GalNAc-Ser/Thr and NeuAc→GalNAc-Ser/Thr, together with the fact that galactose is an inhibitor of the enzyme, suggests that a non-reducing galactose terminus is necessary for recognition of the substrate by the enzyme [3]. The enzyme cannot release Gal→GalNAc from asialo (GM1) ganglioside, which suggests that the β-N-acetylgalactosaminyl linkage is not recognized by the enzyme [3]. |
| Links to other databases: |
BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 59793-96-3 |
| References: |
| 1. |
Bhavanandan, V.P., Umemoto, J. and Davidson, E.A. Characterization of an endo-α-N-acetyl galactosaminidase from Diplococcus pneumoniae. Biochem. Biophys. Res. Commun. 70 (1976) 738–745. [PMID: 7253] |
| 2. |
Endo, Y. and Kibata, A. Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae. J. Biochem. (Tokyo) 80 (1976) 1–8. [PMID: 9374] |
| 3. |
Umemoto, J., Bhavanandan, V.P. and Davidson, E.A. Purification and properties of an endo-α-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae. J. Biol. Chem. 252 (1977) 8609–8614. [PMID: 21877] |
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| [EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008] |
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