| IED ID | IndEnz0002009604 |
| Enzyme Type ID | protease009604 |
| Protein Name |
Xaa-Pro dipeptidyl-peptidase EC 3.4.14.11 X-Pro dipeptidyl-peptidase X-prolyl-dipeptidyl aminopeptidase X-PDAP |
| Gene Name | pepX |
| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Enzyme Sequence | MRFNHFSIVDKNFDEQLAELDQLGFRWSVFWDEKKILKDFLIQSPSDMTALQATAELDVIEFLKSSIELDWEIFWNIALQLLDFVPNFDFEIGKAFEYAKNSNLPQIEAEMTTENIISAFYYLLCTRRKTGMILVEHWVSEGLLPLDNHYHFFNDKSLATFDSSLLEREVLWVESPVDSEQRGENDLIKIQIIRPKSTEKLPVVMTASPYHLGINDKANDLALHDMNVELEEKTSHEIHVEQKLPQKLSAKAKELPIVDKAPYRFTHGWTYSLNDYFLTRGFASIYVAGVGTRSSDGFQTSGDYQQIYSMTAVIDWLNGRARAYTSRKKTHEIKASWANGKVAMTGKSYLGTMAYGAATTGVEGLELILAEAGISSWYNYYRENGLVRSPGGFPGEDLDVLAALTYSRNLDGADFLKGNAEYEKRLAEMTAALDRKSGDYNQFWHDRNYLINTDKVKADVLIVHGLQDWNVTPEQAYNFWKALPEGHAKHAFLHRGAHIYMNSWQSIDFSETINAYFVAKLLDRDLNLNLPPVILQENSKDQVWTMMNDFGANTQIKLPLGKTAVSFAQFDNNYDDETFKKYSKDFNVFKKDLFENKANEAVIDLELPSMLTINGPVELELRLKLNDTKGFLSAQILDFGQKKRLEDKVRVKDFKVLDRGRNFMLDDLVELPLVESPYQLVTKGFTNLQNQSLLTVSDLKADEWFTIKFELQPTIYHLEKADKLRVILYSTDFEHTVRDNRKVTYEIDLSQSKLIIPIESVKN |
| Enzyme Length | 763 |
| Uniprot Accession Number | P22346 |
| Absorption | |
| Active Site | ACT_SITE 348; /note=Charge relay system; /evidence=ECO:0000269|PubMed:1459244; ACT_SITE 468; /note=Charge relay system; ACT_SITE 498; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11; |
| DNA Binding | |
| EC Number | 3.4.14.11 |
| Enzyme Function | FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (36); Chain (1); Helix (24); Sequence conflict (7); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1LNS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 87,697 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.11;3.4.14.5; |