| IED ID | IndEnz0002000588 |
| Enzyme Type ID | protease000588 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT |
| Organism | Lactobacillus helveticus (Lactobacillus suntoryeus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus helveticus (Lactobacillus suntoryeus) |
| Enzyme Sequence | MEYPNLLPRFLKYVKVNSRSDENSDRFPSTEREENFQKNVIMKDLEELGLSDIHYNQKAGSVIAEIPSNVDYDVPVMGFLAHSDTADFNSENVKPQIHKNYDGESKIQLGDSEFYLDPEVYPNLRKYKGQTIITASGDTLLGADDKCGISELMTFAEYLMNHPEVKHGKIRLAFTPDEEIGTGAEQFDVKDFGADFAFTVDGEAPGKLGDCTFSAAQFTLDIQGVNVHPAVAKGQMINAVQVGIDFHNQLPEHDRPEHTDGREGFFHLLSFDGTVDHAHLAYIIRDFERDGLEERKNLVKSIVKKMNDEFGTERIKLQMNDQYYNMADELKKHMDIVDLARDAYKAEGLEVNEDPVRGGTDGSQLTYMGLPCPNIFAGEENMHGRYEYTVLESMYKTVDVMIKMAELNAERAK |
| Enzyme Length | 413 |
| Uniprot Accession Number | Q9L4G1 |
| Absorption | |
| Active Site | ACT_SITE 84; /evidence=ECO:0000250; ACT_SITE 178; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Totally inhibited by EDTA, EGTA, and 1,10-phenanthroline. Strongly inhibited by divalent cations such as Cu(2+), Cd(2+), Co(2+) and Mn(2+). Partially inhibited by the reducing agents 2-mercaptoethanol and dithiothreitol. {ECO:0000269|PubMed:10653753}. |
| 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. Shows broad substrate specificity, exhibiting maximum activity against hydrophobic tripeptides, with the highest activity for Met-Gly-Gly. Therefore this enzyme may play an important role in flavor formation during cheese ripening. Is also able to slowly hydrolyze some hydrophobic dipeptides, but displays no activity against tetrapeptides and the tripeptide Phe-Gly-Gly. {ECO:0000269|PubMed:10653753}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-37 degrees Celsius. Thermolabile. Approximately 45% of the activity remains after incubation for 15 min at 45 degrees Celsius. {ECO:0000269|PubMed:10653753}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Highly active from pH 6 to 8. {ECO:0000269|PubMed:10653753}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Frameshift (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,681 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 mM for tripeptide Met-Gly-Gly {ECO:0000269|PubMed:10653753}; KM=0.6 mM for tripeptide Leu-Gly-Gly {ECO:0000269|PubMed:10653753}; Vmax=80.2 umol/min/ug enzyme with Met-Gly-Gly as substrate {ECO:0000269|PubMed:10653753}; Vmax=6.8 umol/min/ug enzyme with Leu-Gly-Gly as substrate {ECO:0000269|PubMed:10653753}; |
| Metal Binding | METAL 82; /note=Zinc 1; /evidence=ECO:0000250; METAL 144; /note=Zinc 1; /evidence=ECO:0000250; METAL 144; /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 | 3.4.11.4; |