Glycoside Hydrolase Family 89

Known Activitiesα-N-acetylglucosaminidase (EC 3.2.1.50)
Mechanism Retaining
3D Structure Status( β / α ) 8
Catalytic Nucleophile/BaseGlu
Catalytic Proton DonorGlu
External resourcesCAZypedia; InterPro; PFAM;
Statistics GenBank accession (120); Uniprot accession (57); PDB accession (4); 3D entries (1); cryst (0)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 α-N-acetylglucosaminidase (CPF_0859) 3.2.1.50 Clostridium perfringens ATCC 13124 ABG84150.1 Q0TST1 2VC9[A]
2VCA[A]
2VCB[A]
2VCC[A]
 α-N-acetylglucosaminidase (AgnC;CPE0866) 3.2.1.50 Clostridium perfringens str. 13 BAB80572.1
BAI70446.1
NP_561782.1
Q8XM24  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 α-N-acetylglucosaminidase (Sanfilippo disease IIIB) (NAGLU) 3.2.1.50 Homo sapiens AAB06188.1
AAB36604.1
AAB36605.1
AAC50512.1
AAC50513.1
AAH53991.1
ACM85779.1
BAD92767.1
NP_000254.1
NP_000254.2
P54802
Q14769
 
 α-N-acetylglucosaminidase (Naglu) 3.2.1.50 Mus musculus AAB88084.1
AAC26842.1
AAH55733.1
AAM21194.1
BAE37639.1
BAE42009.1
CAM24462.1
NP_038820.1
O54752
O88325
 

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.





Last update: 2012-01-31 © Copyright 1998-2012
AFMB - CNRS - Universités Aix-Marseille I & II