| IED ID | IndEnz0009000104 |
| Enzyme Type ID | chitinase000104 |
| Protein Name |
Di-N-acetylchitobiase EC 3.2.1.- Fragment |
| Gene Name | CTBS CTB |
| Organism | Bos taurus (Bovine) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MARLQLAGSRRLVPLPRRAPRLAPLLLPLLLALPDGARADCPCKVPALCRPMTHRPDFEVFVFNVGHKTWKYYDWSQITTVVLFLKYDPELMCHAHAKGARVVLKGDVPVKDIINATFRASWIAQQVKLAKTQYMDGINLDIEQDVAHSSPEYYALTALVKETTDSFHHEIKGSQ |
| Enzyme Length | 175 |
| Uniprot Accession Number | Q01458 |
| Absorption | |
| Active Site | ACT_SITE 143; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.2.1.- |
| Enzyme Function | FUNCTION: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (1); Non-terminal residue (1); Signal peptide (1) |
| Keywords | Glycoprotein;Glycosidase;Hydrolase;Lysosome;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..38; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,761 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |