IED ID | IndEnz0002000248 |
Enzyme Type ID | protease000248 |
Protein Name |
Peptidase E EC 3.4.13.21 Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E |
Gene Name | pepE STM4190 |
Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Enzyme Sequence | MELLLLSNSTLPGKAWLEHALPLIANQLNGRRSAVFIPFAGVTQTWDEYTDKTAEVLAPLGVNVTGIHRVADPLAAIEKAEIIIVGGGNTFQLLKESRERGLLAPMADRVKRGALYIGWSAGANLACPTIRTTNDMPIVDPNGFDALDLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELTVIGLPEGNWIQVSNGQAVLGGPNTTWVFKAGEEAVALEAGHRF |
Enzyme Length | 229 |
Uniprot Accession Number | P36936 |
Absorption | |
Active Site | ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10762256; ACT_SITE 135; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10762256; ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000269|PubMed:10762256 |
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; |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (14); Chain (1); Helix (8); Natural variant (2); Turn (1) |
Keywords | 3D-structure;Cytoplasm;Dipeptidase;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (4) |
Cross Reference PDB | 1FY2; 1FYE; 6A4R; 6A4S; |
Mapped Pubmed ID | 30194851; |
Motif | |
Gene Encoded By | |
Mass | 24,769 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.13.21; |