Glikopeptidna alfa-N-acetilgalaktozaminidaza
| Glikopeptidna alfa-N-acetilgalaktozaminidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.97 | ||||||||
| CAS broj | 59793-96-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Glikopeptidna alfa-N-acetilgalaktozaminidaza (EC 3.2.1.97, endo-alfa-acetilgalaktozaminidaza, endo-alfa-N-acetil-D-galaktozaminidaza, mucinaminilserin mucinaminidaza, D-galaktozil-3-(N-acetil-alfa-D-galaktozaminil)-L-serin mucinaminohidrolaza, endo-alfa-GalNAc-aza, glikopeptid alfa-N-acetilgalaktozaminidaza, D-galaktozil-N-acetil-alfa-D-galaktozamin D-galaktozil-N-acetil-galaktozaminohidrolaza) je enzim sa sistematskim imenom glikopeptid-D-galaktozil-N-acetil-alfa-D-galaktozamin D-galaktozil-N-acetil-galaktozaminohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 3-O-beta-D-galaktozil-N-acetil-alfa-D-galaktozaminil-L-serin-[protein] + H2O 3-O-beta-D-galaktozil-N-acetil-alfa-D-galaktozamin + L-serin-[protein]
Ovaj enzim katalizuje odvajanje Gal-(1->3)-beta-GalNAc alfa-vezanog za ostatke serina ili treonina u glikoproteinima mucinskog-tipa.
- ↑ 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: 727-734. PMID 18559962.
- ↑ Koutsioulis, D., Landry, D. and Guthrie, E.P. (2008). „Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity”. Glycobiology 18: 799-805. PMID 18635885.
- ↑ 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: 37415-37422. PMID 16141207.
- ↑ 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: 389-398. PMID 19502354.
- ↑ 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: 133-135. PMID 19194003.
- ↑ 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: 394-400. PMID 10620364.
- ↑ 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: 441-446. PMID 18725192.
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