| IED ID | IndEnz0002000264 |
| Enzyme Type ID | protease000264 |
| Protein Name |
Peptidase E EC 3.4.13.21 Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E |
| Gene Name | pepE SF4087 S3643 |
| Organism | Shigella flexneri |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
| Enzyme Sequence | MELLLLSNSTLPGKAWLEHALPLIAEQLQGRRSAVFIPFAGVTQTWDDYTEKTAAVLAPLGVSVTGIHSVVDPVAAIENAEIVIVGGGNTFQLLKQCRERGLLAPITDVVKRGALYIGWSAGANLACPTIRTTNDMPIVDPQGFDALNLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELTIIGLPEGNWITVSKGHATLGGPNTTYVFKAGEEAVPLEAGHRF |
| Enzyme Length | 229 |
| Uniprot Accession Number | Q83PB5 |
| Absorption | |
| Active Site | ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 135; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.; EC=3.4.13.21; Evidence={ECO:0000255|HAMAP-Rule:MF_00510}; |
| DNA Binding | |
| EC Number | 3.4.13.21 |
| Enzyme Function | FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. {ECO:0000255|HAMAP-Rule:MF_00510}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Cytoplasm;Dipeptidase;Hydrolase;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00510}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,628 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |