Detail Information for IndEnz0002000248
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;