| IED ID | IndEnz0002000594 |
| Enzyme Type ID | protease000594 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT |
| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Enzyme Sequence | MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIQLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNMMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPLIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIAPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVAK |
| Enzyme Length | 413 |
| Uniprot Accession Number | P0C2T7 |
| Absorption | |
| Active Site | ACT_SITE 83; /evidence=ECO:0000250; ACT_SITE 178; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, by the reducing agents dithiothreitol and 13-mercaptoethanol, and by the divalent cation Cu(2+). {ECO:0000269|PubMed:16348224}. |
| 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. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides. {ECO:0000269|PubMed:16348224}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:16348224}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16348224}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6); Natural variant (4) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,960 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for tripeptide Leu-Leu-Leu {ECO:0000269|PubMed:16348224}; Vmax=151 umol/min/mg enzyme with Leu-Leu-Leu as substrate {ECO:0000269|PubMed:16348224}; |
| Metal Binding | METAL 81; /note=Zinc 1; /evidence=ECO:0000250; METAL 143; /note=Zinc 1; /evidence=ECO:0000250; METAL 143; /note=Zinc 2; /evidence=ECO:0000250; METAL 179; /note=Zinc 2; /evidence=ECO:0000250; METAL 201; /note=Zinc 1; /evidence=ECO:0000250; METAL 383; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |