Detail Information for IndEnz0002000235
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