EC number:3.2.1.97
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.2 Glycosylases |
| 3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
| ID: | 3.2.1.97 |
|---|---|
| Description: | Endo-alpha-N-acetylgalactosaminidase. |
| Alternative Name: |
Mucinaminylserine mucinaminidase. Glycopeptide alpha-N-acetylgalactosaminidase. Endo-alpha-N-acetyl-D-galactosaminidase. Endo-alpha-GalNAc-ase. Endo-alpha-acetylgalactosaminidase. galactosaminohydrolase. D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl- mucinaminohydrolase. D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine |
| Cath: | 1.10.287.20; 1.10.287.2060; 1.20.1270.70; 3.20.20.80; 2.60.120.260; 2.60.120.870; 2.60.40.1180; 2.70.98.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.2.1.97 |
| BRENDA Enzyme Link: | BRENDA 3.2.1.97 |
| KEGG Enzyme Link: | KEGG3.2.1.97 |
| BioCyc Enzyme Link: | BioCyc 3.2.1.97 |
| ExPASy Enzyme Link: | ExPASy3.2.1.97 |
| EC2PDB Enzyme Link: | EC2PDB 3.2.1.97 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.2.1.97 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.2.1.97 |
| IntEnz Enzyme Link: | IntEnz 3.2.1.97 |
| MEDLINE Enzyme Link: | MEDLINE 3.2.1.97 |
| RHEA:54540 | H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] = beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + L-threonyl-[protein] |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:6].[*:5]-[OH;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. | Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, Fushinobu S | 2009 Sep | 19502354 |
| Novel endo-alpha-N-acetylgalactosaminidases with broader substrate specificity. | Koutsioulis D, Landry D, Guthrie EP | 2008 Oct | 18635885 |
| Characterization of two different endo-alpha-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. | Ashida H, Maki R, Ozawa H, Tani Y, Kiyohara M, Fujita M, Imamura A, Ishida H, Kiso M, Yamamoto K | 2008 Sep | 18559962 |
| RHEA:30983 | H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] = beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + L-seryl-[protein] |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[OH2;+0:5]>>[*:1]-[CH2;+0:2]-[OH;+0:5].[*:4]-[OH;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. | Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, Fushinobu S | 2009 Sep | 19502354 |
| Novel endo-alpha-N-acetylgalactosaminidases with broader substrate specificity. | Koutsioulis D, Landry D, Guthrie EP | 2008 Oct | 18635885 |
| Characterization of two different endo-alpha-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. | Ashida H, Maki R, Ozawa H, Tani Y, Kiyohara M, Fujita M, Imamura A, Ishida H, Kiso M, Yamamoto K | 2008 Sep | 18559962 |