| IED ID | IndEnz0002004383 |
| Enzyme Type ID | protease004383 |
| Protein Name |
Isoaspartyl peptidase EC 3.4.19.5 Beta-aspartyl-peptidase EcAIII Isoaspartyl dipeptidase Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta |
| Gene Name | iaaA spt ybiK b0828 JW0812 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFARGMERVSPEIFSTSLRYEQLLAARKEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYREKGDTVATQ |
| Enzyme Length | 321 |
| Uniprot Accession Number | P37595 |
| Absorption | |
| Active Site | ACT_SITE 179; /note=Nucleophile; /evidence=ECO:0000305|PubMed:18323626 |
| 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). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function. {ECO:0000269|PubMed:11988085}.; FUNCTION: May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption. {ECO:0000269|PubMed:11988085}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (13); Chain (2); Helix (11); Initiator methionine (1); Mutagenesis (1); Region (2); Site (1); Turn (4) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Repressed by cysteine, an effect that is attributed to CysB. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity.; PTM: Both subunits undergo further processing at their C-termini. The overexpressed alpha subunit seems to consist of residues 2-161, with an oxidized Met residue and a tightly coordinated Na(+), whereas the overexpressed beta subunit is processed to residue 315 and has 3 oxidized Met residues. Processing of the alpha subunit is inhibited by Zn(2+). |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1JN9; 1K2X; 1T3M; 2ZAK; 2ZAL; 3C17; |
| Mapped Pubmed ID | 10490104; 12906830; 14616088; 16606699; 16725155; 18334484; 7477383; 8846222; 9541410; 9545304; 9685368; 9737998; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,394 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.138 mM for beta-L-Asp-L-Leu {ECO:0000269|PubMed:15265041}; KM=3.9 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, aspartylglucosamides alpha- or gamma-aspartyl dipeptides.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.5;3.5.1.1; |