| IED ID | IndEnz0002001490 |
| Enzyme Type ID | protease001490 |
| Protein Name |
Alpha-lytic protease L1 EC 3.4.21.12 Alpha-lytic endopeptidase L1 Fragments |
| Gene Name | |
| Organism | Lysobacter sp. (strain XL1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Lysobacter unclassified Lysobacter Lysobacter sp. (strain XL1) |
| Enzyme Sequence | VNVLGGIEYSINNATLCSVGFSVRVFNYAEGAVRGLTQGNACMGRGDSGGSWFTLFERQYGL |
| Enzyme Length | 62 |
| Uniprot Accession Number | P85142 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF) and p-chloromercuribenzoate (PCMB). {ECO:0000269|Ref.2}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.; EC=3.4.21.12; Evidence={ECO:0000250|UniProtKB:P00778, ECO:0000269|Ref.2}; |
| DNA Binding | |
| EC Number | 3.4.21.12 |
| Enzyme Function | FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.2}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Active from pH 7.0 to 11.0. {ECO:0000269|Ref.2}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Non-adjacent residues (4); Non-terminal residue (1) |
| Keywords | Antibiotic;Antimicrobial;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,611 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |