| IED ID | IndEnz0002018805 |
| Enzyme Type ID | protease018805 |
| Protein Name |
Isoaspartyl peptidase/L-asparaginase EC 3.4.19.5 Beta-aspartyl-peptidase Isoaspartyl dipeptidase Cleaved into: Isoaspartyl peptidase/L-asparaginase subunit alpha; Isoaspartyl peptidase/L-asparaginase subunit beta |
| Gene Name | all3922 |
| Organism | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Nostocales Nostocaceae Nostoc unclassified Nostoc Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) |
| Enzyme Sequence | MKSQVQPKLIIHGGAGSSLHGKGGLEAVRQTLHAVVEEVYALLLSGVNASVAVVRGCQLLEDEPRFNAGTGSVLQSDGQIRMSASIMDGALGRFSGVINVSRVKNPIELAQFLQNSPDRVLSDYGSAELAREMQIPSYNALTELRLQEWIQERQDNFKRTMAGVIAEPELLETSNAGRGTIGVVALDTYGKLAVGTSTGGKGFERIGRVSDSAMPAGNYATSYAAVSCTGIGEDIIDECLAPKIVIRVTDGLSLQDSMQRSFAEAHDNKRDFGAIALDANGAIAWGKTCDIILAAFHDGEKIGDTLELAVGTQVGSIS |
| Enzyme Length | 318 |
| Uniprot Accession Number | Q8YQB1 |
| Absorption | |
| Active Site | ACT_SITE 180; /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). Probably performs the final step in the degradation of the reserve polymer cyanophycin (depolymerizes the building block L-beta-Asp-Arg). Also has L-asparaginase activity. {ECO:0000269|PubMed:11988085}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2); Site (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Hydrolase;Protease;Reference proteome |
| 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,638 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.0 mM for L-Asn; KM=1.54 mM for L-beta-Asp-Ala; KM=0.27 mM for L-beta-Asp-Arg; KM=0.52 mM for L-beta-Asp-Gly; KM=0.26 mM for L-beta-Asp-Leu; KM=0.53 mM for L-beta-Asp-Lys; KM=0.68 mM for L-beta-Asp-Phe; Vmax=2.2 umol/min/mg enzyme with L-Asn as substrate; Vmax=12.3 umol/min/mg enzyme with L-beta-Asp-Ala as substrate; Vmax=5.7 umol/min/mg enzyme with L-beta-Asp-Arg as substrate; Vmax=2.7 umol/min/mg enzyme with L-beta-Asp-Gly as substrate; Vmax=4.5 umol/min/mg enzyme with L-beta-Asp-Leu as substrate; Vmax=22.2 umol/min/mg enzyme with L-beta-Asp-Lys as substrate; Vmax=20.1 umol/min/mg enzyme with L-beta-Asp-Phe as substrate; Note=Enzyme is inactive on alpha-aspartyl dipeptides.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |