| IED ID | IndEnz0002001232 |
| Enzyme Type ID | protease001232 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | fpaP |
| Organism | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Weeksellaceae Elizabethkingia Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
| Enzyme Sequence | MIPITTPVGNFKVWTKRFGTNPKIKVLLLHGGPAMTHEYMECFETFFQREGFEFYEYDQLGSYYSDQPTDEKLWNIDRFVDEVEQVRKAIHADKENFYVLGNSWGGILAMEYALKYQQNLKGLIVANMMASAPEYVKYAEVLSKQMKPEVLAEVRAIEAKKDYANPRYTELLFPNYYAQHICRLKEWPDALNRSLKHVNSTVYTLMQGPSELGMSSDARLAKWDIKNRLHEIATPTLMIGARYDTMDPKAMEEQSKLVQKGRYLYCPNGSHLAMWDDQKVFMDGVIKFIKDVDTKSFN |
| Enzyme Length | 298 |
| Uniprot Accession Number | O05420 |
| Absorption | |
| Active Site | ACT_SITE 103; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P96084; ACT_SITE 244; /evidence=ECO:0000250|UniProtKB:O32449; ACT_SITE 271; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P96084 |
| 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:8951032}; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA. {ECO:0000269|PubMed:8951032}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Maximum activity at 42 degrees Celsius. Stable at temperatures up to 44 degrees Celsius, showing 50% of activity after incubation at this temperature for 15 minutes (at pH 8.0). {ECO:0000269|PubMed:8951032}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH 8.0. {ECO:0000269|PubMed:8951032}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,613 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |