IED ID | IndEnz0002000261 |
Enzyme Type ID | protease000261 |
Protein Name |
Peptidase E EC 3.4.13.21 Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E |
Gene Name | pepE SbBS512_E4515 |
Organism | Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella boydii Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) |
Enzyme Sequence | MELLLLSNSTLPGKAWLEHALPLIAEQLQGRRSAVFIPFAGVTQTWDDYTAKTAAVLAPLGVSVTGIHSVVDPVAAIENAEIVIVGGGNTFQLLKQCRERGLLAPITDVVKRGALYIGWSAGANLACPTIRTTNDMPIVDPQGFDALNLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELTIIGLPEGNWITVSKGHATLGGPNTTYVFKAGEEAVPLEAGHRF |
Enzyme Length | 229 |
Uniprot Accession Number | B2TX41 |
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;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 | 24,570 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |