IED ID | IndEnz0002009528 |
Enzyme Type ID | protease009528 |
Protein Name |
Beta-lytic metalloendopeptidase EC 3.4.24.32 Beta-lytic protease |
Gene Name | |
Organism | Lysobacter enzymogenes |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Lysobacter Lysobacter enzymogenes |
Enzyme Sequence | SPNGLLQFPFPRGASWHVGGAHTNTGSGNYPMSSLDMSRGGGSNQNGNWVSASAAGGSFKRHSSCFAEIVHTGGWSTTYYHLMNIQYNTGANVSMNTAIANAPNTQAQALCNGGQSTGPHQHWSLKQNGSFYHLNGTYLSGYRITATGSSYDTNCSRFYLTKNGQNYCYGYYVNPGPN |
Enzyme Length | 178 |
Uniprot Accession Number | P00801 |
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) |
Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
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 | 19,100 |
Kinetics | |
Metal Binding | METAL 120; /note=Zinc; /evidence=ECO:0000255; METAL 122; /note=Zinc; /evidence=ECO:0000255 |
Rhea ID | |
Cross Reference Brenda |