| IED ID | IndEnz0002013112 |
| Enzyme Type ID | protease013112 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | pepIP |
| Organism | Lactobacillus delbrueckii subsp. bulgaricus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus delbrueckii Lactobacillus delbrueckii subsp. bulgaricus |
| Enzyme Sequence | MMQITEKYLPFGNWQTYCRIVGEATDRAPLLLLHGGPGSSHNYFEVLDQVAEKSGRQVIMYDQLGCGNSSIPDDQAETAYTAQTWVKELENVREQLGLDQIHLLGQSWGGMLALIYLCDYQPEGVKSLILSSTLASAKLWSQELHRLIKYLPKGEQAAIKEAETTGNYDSLAYQAANAHFMDQHAIKLTPDLPEPVLRKKKGGSLAYLTGWGPNEYTPIGNLHGYEYTDRLKDLHLPALITSGTDDLCTPLVAKSMYDNLPNARWELFAGCGHMPFVQENAKYQELLSDWLISQD |
| Enzyme Length | 295 |
| Uniprot Accession Number | P46544 |
| Absorption | |
| Active Site | ACT_SITE 107; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 246; /evidence=ECO:0000250; ACT_SITE 273; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited strongly by 3,4-dichloroisocoumarin, bestatin and heavy metal ions. Inactivated by p-chloromercuribenzoate, but reactivated by dithiothreitol. {ECO:0000269|PubMed:8012576}. |
| 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:8012575, ECO:0000269|PubMed:8012576, ECO:0000269|PubMed:9989236}; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. Has a high specificity towards di- or tripeptides with proline at the NH(2)-terminal position, but is not able to hydrolyze longer peptides, or peptides with hydroxyproline at the NH(2)-end. Partially hydrolyzes also peptides with alanine, glycine and leucine at the NH(2)-terminal position. {ECO:0000269|PubMed:8012576}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable at temperatures below 40 degrees Celsius. {ECO:0000269|PubMed:8012576, ECO:0000269|PubMed:9989236}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|PubMed:8012576, ECO:0000269|PubMed:9989236}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Mutagenesis (24) |
| Keywords | Aminopeptidase;Direct protein sequencing;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell envelope {ECO:0000269|PubMed:8012575}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,027 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.93 mM for prolyl-pNA (at 30 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:8012576, ECO:0000269|PubMed:9989236}; Vmax=738 mmol/min/mg enzyme with prolyl-pNA as substrate (at 30 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:8012576, ECO:0000269|PubMed:9989236}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |