| IED ID | IndEnz0002011497 |
| Enzyme Type ID | protease011497 |
| Protein Name |
Beta-lytic metalloendopeptidase EC 3.4.24.32 Beta-lytic protease |
| Gene Name | |
| Organism | Achromobacter lyticus |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Alcaligenaceae Achromobacter Achromobacter lyticus |
| Enzyme Sequence | MKKISKAGLGLALVCALATIGGNAARRATAQRRGSGVFYDEMFDFDIDAHLAKHAPHLHKHSEEISHWAGYSGISRSVDRADGAAERAVTPSARRIVRSASWRAPTASARRPARSRWRCASRCTSAIPTRQGAGDAGPRQSAAGAVRAFRRQRAGGRAARRRRVPAGLRPPVQRTAPGQGGFGPLRQGRPGRAAVSPNGLLQFPFPRGASWHVGGAHTNTGSGNYPMSSLDMSRGGGWGSNQNGNWVSASAAGSFKRHSSCFAEIVHTGGWSTTYYHLMNIQYNTGANVSMNTAIANPANTQAQALCNGGQSTGPHEHWSLKQNGSFYHLNGTYLSGYRITATGSSYDTNCSRFYLTKNGQNYCYGYYVNPGPN |
| Enzyme Length | 374 |
| Uniprot Accession Number | P27458 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO(3)H).; EC=3.4.24.32; |
| DNA Binding | |
| EC Number | 3.4.24.32 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (2); Metal binding (2); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;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 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,085 |
| Kinetics | |
| Metal Binding | METAL 316; /note=Zinc; /evidence=ECO:0000255; METAL 318; /note=Zinc; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |