| IED ID | IndEnz0002014352 |
| Enzyme Type ID | protease014352 |
| Protein Name |
Isoaspartyl peptidase/L-asparaginase LlA EC 3.4.19.5 L-asparagine amidohydrolase Potassium-independent L-asparaginase Cleaved into: Isoaspartyl peptidase/L-asparaginase subunit alpha; Isoaspartyl peptidase/L-asparaginase subunit beta |
| Gene Name | |
| Organism | Lupinus luteus (European yellow 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 luteus (European yellow lupine) |
| Enzyme Sequence | MGGWSIALHGGAGDIPFSLPPERRKPREEGLRHCLQIGVEALKAQKPPLDVVELVVRELENIEHFNAGIGSVLTNSGTVEMEASIMDGNTMKCGAVSGLSTVLNPISLARLVMDKTPHIYLAFQGAQDFAKQQGVETVDSSHLITAENVERLKLAIEANRVQVDYSQYNYPEPVKDDAEKELPLTNGDSQIGTVGCVAVDSHGNLASATSTGGLVNKMVGRIGDTPLIGAGTYANELCAVSATGKGEEIIRATVARDVAALMEFKGLSLKEAADFVIHERTPKGTVGLIAVSAAGEIAMPFNTTGMFRACATEDGYSEIAIWPTT |
| Enzyme Length | 325 |
| Uniprot Accession Number | Q9ZSD6 |
| 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: Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Also has L-asparaginase activity, which is used to liberate stored nitrogen during seed development. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (2); Helix (9); Region (2); Site (1); Turn (2) |
| Keywords | 3D-structure;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. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2GEZ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,449 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.136 mM for beta-L-Asp-L-Leu {ECO:0000269|PubMed:15265041}; KM=4.8 mM for L-Asn {ECO:0000269|PubMed:15265041}; Note=No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln or aspartylglucosamides.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.5; |