| IED ID | IndEnz0002012939 |
| Enzyme Type ID | protease012939 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | pip pepI |
| Organism | Lactobacillus helveticus (Lactobacillus suntoryeus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus helveticus (Lactobacillus suntoryeus) |
| Enzyme Sequence | MEIIEGKMPFMGYETYYRIVGERSEKPPLVLLHGGPGSSHNYFEVLDELAQKDGRRIIMYDQLGCGESSIPDDHPELYTKETWVKELEALREHLALRKMHLLGQSWGGMLAIIYMCDYHPEGIQSLILSSTLSSASLWSKELHRMIKYLPIEEQAAIHRAELTGNFNDPDYLKANEHFMNQHAIDMTKTWPECVMRKKRGGTVAYETAWGPNEYTPEGNLHDYEYTDKLSKIKVPTLITSGTDDLCTPYVAKTMQDQIASSKWRLFEGCGHMSFVEKTDEYVALLQEWLDQHDE |
| Enzyme Length | 294 |
| Uniprot Accession Number | P52278 |
| Absorption | |
| Active Site | ACT_SITE 105; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 244; /evidence=ECO:0000250; ACT_SITE 271; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000269|PubMed:9004508}; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. Hydrolyzes only di- and tripeptides with proline in the first position. {ECO:0000269|PubMed:9004508}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum activity at 40 degrees Celsius. {ECO:0000269|PubMed:9004508}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. At pH values above 7.5, the activity sharply decreases. {ECO:0000269|PubMed:9004508}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell envelope {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,845 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for Pro-pNA (at 40 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:9004508}; Vmax=350 mmol/min/mg enzyme with Pro-pNA as substrate {ECO:0000269|PubMed:9004508}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.5; |