| IED ID | IndEnz0009000165 |
| Enzyme Type ID | chitinase000165 |
| Protein Name |
Beta-hexosaminidase EC 3.2.1.52 Beta-N-acetylhexosaminidase N-acetyl-beta-glucosaminidase NAHA1 Fragment |
| Gene Name | |
| Organism | Palythoa caribaeorum (White encrusting zoanthid coral) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Cnidaria Anthozoa (anthozoans) Hexacorallia Zoantharia (zoanthids) Sphenopidae Palythoa Palythoa caribaeorum (White encrusting zoanthid coral) |
| Enzyme Sequence | GKSSSRPLGDATLGDLDFDIEVTQDYWDDLAR |
| Enzyme Length | 32 |
| Uniprot Accession Number | P85512 |
| Absorption | |
| Active Site | ACT_SITE 21; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | ACTIVITY REGULATION: Activity is decreased by HgCl(2) and maltose. Activity is stimulated by Na(2)SeO(4), BaCl(2), MgCl(2), chondroitin 6-sulfate and phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:18171621}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:18171621}; |
| DNA Binding | |
| EC Number | 3.2.1.52 |
| Enzyme Function | FUNCTION: Preferentially hydrolyzes pNP-GlcNAc, hydrolyzes pNP-GalNAc to a lesser extent. {ECO:0000269|PubMed:18171621}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Has maximum activity at 45 to 60 degrees Celsius. Inactive at temperatures of 70 degrees Celsius and above. {ECO:0000269|PubMed:18171621}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. Active over a broad range of pH values. {ECO:0000269|PubMed:18171621}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Non-terminal residue (2) |
| Keywords | Direct protein sequencing;Glycosidase;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,557 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.53 mM for pNP-GlcNAc {ECO:0000269|PubMed:18171621}; Vmax=88.1 umol/h/mg enzyme with pNP-Glc-NAc as substrate {ECO:0000269|PubMed:18171621}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |