| IED ID | IndEnz0002000682 |
| Enzyme Type ID | protease000682 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT STM1227 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MDKLLERFLHYVSLDTQSKSGVRQVPSTEGQWKLLRLLKQQLEEMGLVNITLSEKGTLMATLPANVEGDIPAIGFISHVDTSPDFSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGVAEIMTALAVLKGNPIPHGDIKVAFTPDEEVGKGAKHFDVEAFGAQWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPADEAPETTEGYEGFYHLASMKGTVDRAEMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDCYIELVIEDSYYNMREKVVEHPHILDIAQQAMRDCHITPEMKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVRIAELTAKRGQ |
| Enzyme Length | 409 |
| Uniprot Accession Number | P26311 |
| Absorption | |
| Active Site | ACT_SITE 80; /evidence=ECO:0000250; ACT_SITE 173; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:6341363}. |
| 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 the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N-blocked or C-blocked tripeptides, and tetrapeptides. {ECO:0000269|PubMed:6341363}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (19); Chain (1); Helix (14); Metal binding (6); Region (3); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1FNO; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,849 |
| Kinetics | |
| Metal Binding | METAL 78; /note=Zinc 1; /evidence=ECO:0000269|PubMed:11856302; METAL 140; /note=Zinc 1; /evidence=ECO:0000269|PubMed:11856302; METAL 140; /note=Zinc 2; /evidence=ECO:0000269|PubMed:11856302; METAL 174; /note=Zinc 2; /evidence=ECO:0000269|PubMed:11856302; METAL 196; /note=Zinc 1; /evidence=ECO:0000269|PubMed:11856302; METAL 379; /note=Zinc 2; /evidence=ECO:0000269|PubMed:11856302 |
| Rhea ID | |
| Cross Reference Brenda |