| IED ID | IndEnz0002005112 |
| Enzyme Type ID | protease005112 |
| Protein Name |
Isoaspartyl peptidase/L-asparaginase EC 3.4.19.5 EC 3.5.1.1 Asparaginase-like protein 1 Asparaginase-like sperm autoantigen Beta-aspartyl-peptidase Glial asparaginase Isoaspartyl dipeptidase L-asparagine amidohydrolase Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain |
| Gene Name | Asrgl1 Alp Gliap Hiob |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MATARPSSCGRDSVPATPRASIDVSLVVVVHGGGASNISPGRKELVSEGIAKAATEGYNILKAGGSAVDAVEGAVTMLENDPEFNAGYGSVLNADGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGRGAEKFAADMGIPQTPAEKLITERTKKHLEKEKLEKGAQKADCPKNSGTVGAVALDCKGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVDEAATLALDYMKSKLKGLGGLILINKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETKTRNLPTC |
| Enzyme Length | 333 |
| Uniprot Accession Number | Q8VI04 |
| Absorption | |
| Active Site | ACT_SITE 191; /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:0000269|PubMed:12753071}; CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000269|PubMed:12753071}; |
| DNA Binding | |
| EC Number | 3.4.19.5; 3.5.1.1 |
| Enzyme Function | FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. 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 (By similarity). May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. {ECO:0000250|UniProtKB:Q7L266, ECO:0000269|PubMed:12753071}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2) |
| Keywords | Autocatalytic cleavage;Cytoplasm;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:12753071}. Note=Midpiece of sperm tail. |
| 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 | 16396496; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,410 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for L-aspartic acid beta-(7-amido-4-methylcoumarin) {ECO:0000269|PubMed:12753071}; |
| Metal Binding | |
| Rhea ID | RHEA:21016 |
| Cross Reference Brenda |