Detail Information for IndEnz0002018469
IED ID IndEnz0002018469
Enzyme Type ID protease018469
Protein Name Asp/Glu-specific dipeptidyl-peptidase
EC 3.4.14.-
Dipeptidyl-peptidase 11
DPP11
Gene Name dpp11 Sputcn32_0757
Organism Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Shewanellaceae Shewanella Shewanella putrefaciens (Pseudomonas putrefaciens) Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Enzyme Sequence MRIALVATLVLTSGIANADEGQWQPYQMPSIADKLSERGIDIPAEKLADLTSYPMNAVVGLGYCTASFVSPQGLVVTNHHCAYKAIQYNTKQEHNYLEQGFLATSMDKEPSAGPNERLYITEAVTDVTKDVTKELSQDPLTRYEEIQNNSKALIKNCEVDDNYRCNVRSFHNGLEYYLIKQLMIRDVRLVYAPPESVGGYGGDIDNYEYPRHSGDFAFLRAYVGKDGKPAAYAEDNIPYKPKSYLKVNADGVKAGDGVFVAGYPGTTSRYNLTSELKFASDWLYPTQAKRYQLQIDTINAMGQEDADIAIKYAGNMASMANRMKKLNGLLAGFKATDIIGIKQSREDNFLAWLKQNPKLNQNLIAELEVLLAEQQQVFQSNYYFTNAQSSTLLTAANSLYRLAKEKQKSDAEREIGYQERDLAMFSSRLKRIDSSFHVDVDKTLWQQDLRAYLAQPNRIAALDDALDLNNKETNLEAKLDGLYSLTTLTDQAQRLAWMDADTTTFETSTDPFIRLAVALYDTNMAQEKAEKILDGKLSTARPDYMAAVIEYYKANNWPVYPDANGTLRISYGMVDGYQSRDALYKQPFTRLDGIVAKHTGAEPYNAPQKLLDAISEQRFGDHLVKSVYQDPRGWICRLFSCLDKPEEFNSVPVNFLSSVDTTGGNSGSPVFNGKGELVGLNFDSTYEAITKDWFFNPTITRAVHVDIRYILWMMDKVDHADNLIKELDLVRN
Enzyme Length 732
Uniprot Accession Number A4Y3F4
Absorption
Active Site ACT_SITE 80; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 666; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.14.-
Enzyme Function FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has probably a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Glu-methylcoumaryl-7-amide (Leu-Glu-MCA) as compared to Leu-Asp-MCA. {ECO:0000269|PubMed:23246913}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Mutagenesis (2); Signal peptide (1)
Keywords Aminopeptidase;Hydrolase;Protease;Serine protease;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 82,383
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda