| IED ID | IndEnz0002014350 |
| Enzyme Type ID | protease014350 |
| Protein Name |
Isoaspartyl peptidase/L-asparaginase EC 3.4.19.5 L-asparagine amidohydrolase Cleaved into: Isoaspartyl peptidase/L-asparaginase subunit alpha; Isoaspartyl peptidase/L-asparaginase subunit beta |
| Gene Name | |
| Organism | Lupinus angustifolius (Narrow-leaved blue lupine) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade genistoids sensu lato core genistoids Genisteae Lupinus Lupinus angustifolius (Narrow-leaved blue lupine) |
| Enzyme Sequence | MGGWSIALHGGAGDIPFSLPPERRQPREEGLRHCLQIGVEALKSQKPPLDVVELVVRELENIQHFNAGIGSVLTNSGTVEMEASIMDGKTMKCGAVSGLSTVLNPISLARLVMDKTPHIYLAFQGAQDFAKQQGVETVDSSHFITAENVERLKLAIEANRVQVDYSQYNYPQPAQDDAEKELPLANGDSQIGTVGCVAVDSHGNLASATSTGGLVNKMVGRIGDTPLIGAGTYANELCAVSATGKGEAIISATVARDVAALMEFKGLSLKEAADYVVHERTPKGTVGLIAVSAAGEIAMPFNTTGMFRASATEDGYSEIAIWPTT |
| Enzyme Length | 325 |
| Uniprot Accession Number | P30364 |
| Absorption | |
| Active Site | ACT_SITE 193; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; |
| DNA Binding | |
| EC Number | 3.4.19.5 |
| Enzyme Function | FUNCTION: Acts in asparagine catabolism but also in the final steps of protein degradation via hydrolysis of a range of isoaspartyl dipeptides. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2); Site (1) |
| Keywords | Autocatalytic cleavage;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| 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 (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,312 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |