| Identification |
|---|
| HMDB Protein ID
| HMDBP13966 |
| Secondary Accession Numbers
| None |
| Name
| Beta-hexosaminidase Amuc_2018 |
| Synonyms
|
- Beta-N-acetylhexosaminidase Am2301
|
| Gene Name
| (GENBANK) BETA-N-ACETYLHEXOSAMINIDASE |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Hydrolyzes terminal GlcNAc residues from terminally unbranched N-glycans and from chitobiose. Hydrolyzes beta-1,6-linked N-acetylglucosamine and beta-1,4-linked N-acetylgalactosamine from pNP-alpha-GalNAc[beta1,3Gal]beta1,6GlcNAc and pNP-beta-GlcNAc-beta1,4-GalNAc substrates, respectively, as well as beta-1,2-linked N-acetylglucosamine units from the non-reducing end of N-glycans. Hydrolyzes GlcNAc residues linked to alpha1,3- or alpha1,6-mannose branch, but has low activity on substrates with more than one GlcNAc residue on one of the mannose branches. Releases terminal GlcNAc moieties from the N-glycopeptide Gly-Glu-Asn-(GlcNAc2Man3GlcNAc2)-Arg with high efficiency. Has moderate hydrolytic activity on the chitobiose moiety of N-glycopeptide substrate Gly-Glu-Asn-(GlcNAc2)-Arg. Does not hydrolyze GlcNAc residues from N-glycan structures bearing a bisecting GlcNAc moiety (beta1,4-linked GlcNAc to the beta1,4-linked core mannose) (PubMed:29304441). Potentially capable of cleaving the specific glycoside linkages in the process of mucin degradation in human intestinal tract (Probable). Hydrolyzes synthetic substrate pNP-beta-GlcNAc with high activity and pNP-beta-GalNAc to a lesser extent (PubMed:29304441, PubMed:30846208). Does not hydrolyze pNP-beta-glucose, pNP-beta-galactose, pNP-alpha-glucose, pNP-alpha-galactose, pNP-alpha-GlcNAc or pNP-alpha-fucose (PubMed:29304441). |
| Pathways
|
- Amino sugar and nucleotide sugar metabolism
- Other glycan degradation
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| carbohydrate metabolic process |
| Molecular Function |
| N-acetyl-beta-D-galactosaminidase activity |
| beta-N-acetylhexosaminidase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 493 |
| Molecular Weight
| 56043.64 |
| Theoretical pI
| 8.312 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| B2UP57 |
| UniProtKB/Swiss-Prot Entry Name
| H2018_AKKM8 |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - van Passel MW, Kant R, Zoetendal EG, Plugge CM, Derrien M, Malfatti SA, Chain PS, Woyke T, Palva A, de Vos WM, Smidt H: The genome of Akkermansia muciniphila, a dedicated intestinal mucin degrader, and its use in exploring intestinal metagenomes. PLoS One. 2011 Mar 3;6(3):e16876. doi: 10.1371/journal.pone.0016876. [PubMed:21390229 ]
- Wang M, Zhang XY, Guo RR, Cai ZP, Hu XC, Chen H, Wei S, Voglmeir J, Liu L: Cloning, purification and biochemical characterization of two beta-N-acetylhexosaminidases from the mucin-degrading gut bacterium Akkermansia muciniphila. Carbohydr Res. 2018 Mar 2;457:1-7. doi: 10.1016/j.carres.2017.12.007. Epub 2017 Dec 23. [PubMed:29304441 ]
- Chen X, Wang J, Liu M, Yang W, Wang Y, Tang R, Zhang M: Crystallographic evidence for substrate-assisted catalysis of beta-N-acetylhexosaminidas from Akkermansia muciniphila. Biochem Biophys Res Commun. 2019 Apr 16;511(4):833-839. doi: 10.1016/j.bbrc.2019.02.074. Epub 2019 Mar 4. [PubMed:30846208 ]
|
