IED ID | IndEnz0002000235 |
Enzyme Type ID | protease000235 |
Protein Name |
Peptidase E EC 3.4.13.21 Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E |
Gene Name | pepE PM0454 |
Organism | Pasteurella multocida (strain Pm70) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Pasteurella Pasteurella multocida Pasteurella multocida subsp. multocida Pasteurella multocida (strain Pm70) |
Enzyme Sequence | MKNMLLMSGSKYQNTDYLVHTLPWLQDFLADYQGKTVAFVPYAGVRQSYDEYELKVQKALAELNVAILSVHRAEKHAEIIEKADVIAIGGGNTFCLLKGMYEHHLLPLIREKVQSGTPYFGWSAGANVAGRSIMTTNDMPITYPPSFDALNLFPHQLNPHFISGKPAGHNGESREERLAEFLIVNPTANVYALPEGTALHIQGQQARVLGQHDVLLFSENMQLATLPVNSVFDY |
Enzyme Length | 234 |
Uniprot Accession Number | Q9CNH7 |
Absorption | |
Active Site | ACT_SITE 123; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 138; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 160; /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); Erroneous initiation (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 | 26,058 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |