| IED ID | IndEnz0002002526 |
| Enzyme Type ID | protease002526 |
| Protein Name |
Marinostatin-L Cleaved into: Marinostatin-C1; Marinostatin-C2; Marinostatin-D |
| Gene Name | mstI |
| Organism | Alteromonas sp. (strain B-10-31) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Alteromonadaceae Alteromonas unclassified Alteromonas Alteromonas sp. (strain B-10-31) |
| Enzyme Sequence | MKTTPFFANLLASQTRELTENELEMTAGGTASQQSPVQEVPEQPFATMRYPSDSDEDGFNFPV |
| Enzyme Length | 63 |
| Uniprot Accession Number | P29399 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Inhibits subtilisin, chymotrypsin, and elastase, but not trypsin. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Modified residue (1); Peptide (3); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | 3D-structure;Direct protein sequencing;Protease inhibitor;Pyrrolidone carboxylic acid;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 43; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:1794974 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:9972273 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1IXU; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,986 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |