| IED ID | IndEnz0002019154 |
| Enzyme Type ID | protease019154 |
| 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 | Mus musculus (Mouse) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MACARGTVAPPVRASIDVSLVVVVHGGGASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETRTRDLPC |
| Enzyme Length | 326 |
| Uniprot Accession Number | Q8C0M9 |
| Absorption | |
| Active Site | ACT_SITE 185; /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. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000250|UniProtKB:Q7L266}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Erroneous initiation (1); Frameshift (2); Region (2) |
| Keywords | Autocatalytic cleavage;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}. Note=Midpiece of sperm tail. In retina localizes in photoreceptor inner segment (PubMed:27106100). {ECO:0000250|UniProtKB:Q7L266, ECO:0000269|PubMed:27106100}. |
| 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|UniProtKB:Q7L266}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11217851; 12466851; 14681479; 15033168; 16615898; 19455133; 21267068; 21677750; 9356459; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,950 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21016 |
| Cross Reference Brenda |