Detail Information for IndEnz0002000315
IED ID IndEnz0002000315
Enzyme Type ID protease000315
Protein Name Xaa-Pro dipeptidase
X-Pro dipeptidase
EC 3.4.13.9
Imidodipeptidase
Proline dipeptidase
Prolidase
Gene Name pepQ b3847 JW3823
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MESLASLYKNHIATLQERTRDALARFKLDALLIHSGELFNVFLDDHPYPFKVNPQFKAWVPVTQVPNCWLLVDGVNKPKLWFYLPVDYWHNVEPLPTSFWTEDVEVIALPKADGIGSLLPAARGNIGYIGPVPERALQLGIEASNINPKGVIDYLHYYRSFKTEYELACMREAQKMAVNGHRAAEEAFRSGMSEFDINIAYLTATGHRDTDVPYSNIVALNEHAAVLHYTKLDHQAPEEMRSFLLDAGAEYNGYAADLTRTWSAKSDNDYAQLVKDVNDEQLALIATMKAGVSYVDYHIQFHQRIAKLLRKHQIITDMSEEAMVENDLTGPFMPHGIGHPLGLQVHDVAGFMQDDSGTHLAAPAKYPYLRCTRILQPGMVLTIEPGIYFIESLLAPWREGQFSKHFNWQKIEALKPFGGIRIEDNVVIHENNVENMTRDLKLA
Enzyme Length 443
Uniprot Accession Number P21165
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9;
DNA Binding
EC Number 3.4.13.9
Enzyme Function FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position and a polar or nonpolar amino acid at the N-terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX. {ECO:0000269|PubMed:15313226}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (19); Chain (1); Frameshift (1); Helix (19); Metal binding (7); Turn (3)
Keywords 3D-structure;Dipeptidase;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome
Interact With P33643
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4QR8;
Mapped Pubmed ID 15690043; 16606699; 25354344;
Motif
Gene Encoded By
Mass 50,176
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for Ala-Pro {ECO:0000269|PubMed:15313226}; KM=0.10 mM for Arg-Pro {ECO:0000269|PubMed:15313226}; KM=1.4 mM for Gly-Pro {ECO:0000269|PubMed:15313226}; KM=0.15 mM for His-Pro {ECO:0000269|PubMed:15313226}; KM=0.10 mM for Ile-Pro {ECO:0000269|PubMed:15313226}; KM=1.0 mM for Leu-Pro {ECO:0000269|PubMed:15313226}; KM=0.27 mM for Lys-Pro {ECO:0000269|PubMed:15313226}; KM=0.13 mM for Met-Pro {ECO:0000269|PubMed:15313226}; KM=0.43 mM for Phe-Pro {ECO:0000269|PubMed:15313226}; KM=0.31 mM for Pro-Pro {ECO:0000269|PubMed:15313226}; KM=0.46 mM for Ser-Pro {ECO:0000269|PubMed:15313226}; KM=0.16 mM for Tyr-Pro {ECO:0000269|PubMed:15313226}; KM=0.40 mM for Val-Pro {ECO:0000269|PubMed:15313226}; KM=38 mM for diisopropylfluorophosphate {ECO:0000269|PubMed:15313226}; Note=Among the dipeptides described above, the highest catalytic efficiency is observed with dipeptides containing charge residues.;
Metal Binding METAL 246; /note=Manganese 2; /evidence=ECO:0000250; METAL 257; /note=Manganese 1; /evidence=ECO:0000250; METAL 257; /note=Manganese 2; /evidence=ECO:0000250; METAL 339; /note=Manganese 1; /evidence=ECO:0000250; METAL 384; /note=Manganese 1; /evidence=ECO:0000250; METAL 423; /note=Manganese 1; /evidence=ECO:0000250; METAL 423; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda