IED ID | IndEnz0002016782 |
Enzyme Type ID | protease016782 |
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 | sll0422 |
Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa) |
Enzyme Sequence | MTPKLIIHGGASSLDDKGGLATVRQSLHQIVAAVYETLTAGGSAMDAVVQGCELLENEPRFNAGTGSVLQSDGQVRMSASLMDGDRQNFSGVINVSRIKNPIQMAQFLQGQTDRILSDYGAADLAREMQLPIYDPATDFRIQEWMEERGEDVRKKMARLIADPTVGIEARKGTIGVVALDANGKIAAGTSTGGKGLERIGRVSDSAMPAGNYATRFAGVSCTGVGEDIINECLAAKVVIRVKDGQNLAQAMAKSITEALENNTDLGAIALDHQGHIAWGKTCPVLLAAYHTGTAIGDTLELTDGDHYGNASILKLQKTVKKIQTKTRGK |
Enzyme Length | 329 |
Uniprot Accession Number | P74383 |
Absorption | |
Active Site | ACT_SITE 173; /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 | 34,895 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.66 mM for L-Asn; KM=1.0 mM for L-beta-Asp-Ala; KM=0.32 mM for L-beta-Asp-Arg; KM=1.6 mM for L-beta-Asp-Gly; KM=0.33 mM for L-beta-Asp-Leu; KM=0.55 mM for L-beta-Asp-Lys; KM=0.56 mM for L-beta-Asp-Phe; Vmax=1.6 umol/min/mg enzyme with L-Asn as substrate; Vmax=7.3 umol/min/mg enzyme with L-beta-Asp-Ala as substrate; Vmax=21.0 umol/min/mg enzyme with L-beta-Asp-Arg as substrate; Vmax=2.4 umol/min/mg enzyme with L-beta-Asp-Gly as substrate; Vmax=14.7 umol/min/mg enzyme with L-beta-Asp-Leu as substrate; Vmax=29.4 umol/min/mg enzyme with L-beta-Asp-Lys as substrate; Vmax=23.6 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 |