| IED ID | IndEnz0002000284 |
| Enzyme Type ID | protease000284 |
| Protein Name |
Neutral endopeptidase EC 3.4.24.- Endopeptidase O |
| Gene Name | pepO LACR_D16 |
| Organism | Lactococcus lactis subsp. cremoris (strain SK11) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) Lactococcus cremoris subsp. cremoris Lactococcus lactis subsp. cremoris (strain SK11) |
| Enzyme Sequence | MTRIQDDLFATVNAEWLENAEIPADKPRISAFDELVLKNEKNLAKDLADLSQNLPTDNPELLEAIKFYNKAGDWQAREKADFSAVKNELAKVETLNTFEDFKNNLTQLVFHSQAPLPFSFSVEPDMKDAIHYSLGFSGPGLILPDTTYYNDEHPRKKELLDFWAKNTSEILKTFDVENAEEIAKSALKFDALLVPSANTSEEWAKYAELYHPISTDSFVSKVKNLDLKSLIKDLVKTEPDKVIVYEDRFYESFDSLINEENWSLIKAWMLTKIARGATSFFNEDLRILGGAYGRFLSNVQEARSQEKHQLDLTESYFSQVIGLFYGKKYFGEAGKADVKRMVTAMIKVYQARLSKNEWLSQETAEKAIEKLDAITPFIGFPDKLPEIYSRLKTTSGSLYEDALKFDEILTARTFEKFSEDVDKTSWHMPAHMVNAYYSPDSNTIVFPAAILQAPFYSLEQSSSQNYGGIGTVIAHEISHAFDNNGAQFDKEGNLNKWWLDEDYEAFEEKQKEMIALFDGVETEAGPANGKLIVSENIADQGGITAALTAAKDEKDVDLKAFFSQWAKIWRMKASKEFQQMLLSMDFHAPAKLRANIPPTNLEEFYDTFDVKETDKMYRAPENRLKIW |
| Enzyme Length | 627 |
| Uniprot Accession Number | Q02VB0 |
| Absorption | |
| Active Site | ACT_SITE 476; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 539; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by 1,10-phenanthroline and phosphoramidon but relatively insensitive to EDTA. Not significantly inhibited by p-chloromercuribenzoate nor by phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:8012609}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Endopeptidase with broad substrate specificity for several oligopeptides. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-38 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Initiator methionine (1); Metal binding (3) |
| Keywords | Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Plasmid;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8012609}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pLACR4; Plasmid pSK11L |
| Mass | 71,528 |
| Kinetics | |
| Metal Binding | METAL 475; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 479; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 535; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Rhea ID | |
| Cross Reference Brenda |