| IED ID | IndEnz0002000564 |
| Enzyme Type ID | protease000564 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase Fragment |
| Gene Name | pepT |
| Organism | Fusobacterium nucleatum subsp. polymorphum |
| Taxonomic Lineage | cellular organisms Bacteria Fusobacteria Fusobacteriia Fusobacteriales Fusobacteriaceae Fusobacterium Fusobacterium nucleatum Fusobacterium nucleatum subsp. polymorphum |
| Enzyme Sequence | MDXKXYVDLKERFLRYVKFN |
| Enzyme Length | 20 |
| Uniprot Accession Number | P81207 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the chelating agents EDTA and 1,10-phenanthroline, by bestatin and amastatin, p-hydroxymercuribenzoate and some divalent cations at high concentration. {ECO:0000269|PubMed:9695913}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of the N-terminal residue from a tripeptide.; EC=3.4.11.4; |
| DNA Binding | |
| EC Number | 3.4.11.4 |
| Enzyme Function | FUNCTION: Cleaves a wide range of dipeptides and tripeptides, but does not display activity against larger peptides. May have a role in the survival of F.nucleatum in the subgingival environment of the mouth. {ECO:0000269|PubMed:9695913}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8. {ECO:0000269|PubMed:9695913}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Aminopeptidase;Cobalt;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell envelope {ECO:0000269|PubMed:9695913}. Note=Cell envelope associated. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,587 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.66 mM for dipeptide Leu-Ala {ECO:0000269|PubMed:9695913}; KM=4.0 mM for tripeptide Leu-Gly-Gly {ECO:0000269|PubMed:9695913}; Vmax=0.12 umol/min/mg enzyme with Leu-Ala as substrate {ECO:0000269|PubMed:9695913}; Vmax=0.09 umol/min/mg enzyme with Leu-Gly-Gly as substrate {ECO:0000269|PubMed:9695913}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |