| IED ID | IndEnz0002015658 |
| Enzyme Type ID | protease015658 |
| Protein Name |
Neutral protease EC 3.4.24.25 Aeromonolysin Vibriolysin |
| Gene Name | nprV |
| Organism | Vibrio proteolyticus (Aeromonas proteolytica) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio proteolyticus (Aeromonas proteolytica) |
| Enzyme Sequence | MNKTQRHINWLLAVSAATALPVTAAEMINVNDGSLLNQALKAQSQSVAPVETGFKQMKRVVLPNGKVKVRYQQTHHGLPVFNTSVVATESKSGSSEVFGVMAQGIADDVSTLTPSVEMKQAISIAKSRFQQQEKMVAEPATENEKAELMVRLDDNNQAQLVYLVDFFVAEDHPARPFFFIDAQTGEVLQTWDGLNHAQADGTGPGGNTKTGRYEYGSDFPPFVIDKVGTKCSMNNSAVRTVDLNGSTSGNTTYSYTCNDSTNYNDYKAINGAYSPLNDAHYFGKVVFDMYKDWMNTTPLTFQLTMRVHYGNNYENAFWNGSSMTFGDGYSTFYPLVDINVSAHEVSHGFTEQNSGLVYENMSGGMNEAFSDIAGEAAEFYMKGSVDWVVGADIFKSSGGLRYFDQPSRDGRSIDHASDYYNGLNVHYSSGVFNRAFYLLANKAGWDVRKGFEVFTLANQLYWTANSTFDEGGCGVVKAASDMGYSVADVEDAFNTVGVNASCGATPPPSGDVLEIGKPLANLSGNRNDMTYYTFTPSSSSSVVIKITGGTGDADLYVKAGSKPTTTSYDCRPYKYGNEEQCSISAQAGTTYHVMLRGYSNYAGVTLRAD |
| Enzyme Length | 609 |
| Uniprot Accession Number | Q00971 |
| Absorption | |
| Active Site | ACT_SITE 344; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 426; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.; EC=3.4.24.25; |
| DNA Binding | |
| EC Number | 3.4.24.25 |
| Enzyme Function | FUNCTION: Extracellular zinc metalloprotease. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 66,363 |
| Kinetics | |
| Metal Binding | METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 347; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 367; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.25; |