| IED ID | IndEnz0002014577 |
| Enzyme Type ID | protease014577 |
| Protein Name |
Isoaspartyl peptidase/L-asparaginase EC 3.4.19.5 EC 3.5.1.1 Asparaginase-like protein 1 Beta-aspartyl-peptidase Isoaspartyl dipeptidase L-asparagine amidohydrolase Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain |
| Gene Name | asrgl1 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MKPVIVVHGGAGKIVEELDATYRAGVKRAVLKGYDVLSQGGSALTAVEEAVIVLEDEQIFNAGHGSVLNEKGDIEMDAIIMDGKNLDSGAVSAIRNIANPIKLARLVMEKTDHMLLTCEGATLFAKAQGIPEVPNESLVTERSRKRWMKNLKENSNPVADQIGLGTVGAVAIDCEGNVACATSTGGLTNKMVGRVGDTACIGSGGYADNNVGAVSTTGHGESIMKVILARLILHHMEQGKSPEEAADAGLNYMKSRVGGIGGVIIVNSSGDWTAKFSTNQMSWAAVKDDQLHIGIYHGENNVTPLEKAL |
| Enzyme Length | 309 |
| Uniprot Accession Number | Q6GM78 |
| Absorption | |
| Active Site | ACT_SITE 166; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000250|UniProtKB:Q7L266}; CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266}; |
| DNA Binding | |
| EC Number | 3.4.19.5; 3.5.1.1 |
| Enzyme Function | FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2) |
| Keywords | Autocatalytic cleavage;Cytoplasm;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,505 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21016 |
| Cross Reference Brenda |