IED ID | IndEnz0002000596 |
Enzyme Type ID | protease000596 |
Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase hTPepTR |
Gene Name | pepT |
Organism | Lactococcus lactis subsp. hordniae |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis Lactococcus lactis subsp. hordniae |
Enzyme Sequence | MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIKLGDTEFTLDPKDFPSLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLAEYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNTMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAEFGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIVPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVVK |
Enzyme Length | 413 |
Uniprot Accession Number | Q84BV2 |
Absorption | |
Active Site | ACT_SITE 83; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; ACT_SITE 178; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_00550 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of the N-terminal residue from a tripeptide.; EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689}; |
DNA Binding | |
EC Number | 3.4.11.4 |
Enzyme Function | FUNCTION: Cleaves the N-terminal amino acid of tripeptides. {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is slightly lower than 40 degrees Celsius. {ECO:0000269|PubMed:15752689}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 8. {ECO:0000269|PubMed:15752689}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (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:0000255|HAMAP-Rule:MF_00550}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,993 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 639 sec(-1) with GGF tripeptide as substrate. kcat is 915 sec(-1) with GGA tripeptide as substrate. kcat is 1015 sec(-1) with GAA tripeptide as substrate. kcat is 1219 sec(-1) with GAY tripeptide as substrate. kcat is 373 sec(-1) with AAA tripeptide as substrate. kcat is 1640 sec(-1) with AAG tripeptide as substrate. {ECO:0000269|PubMed:15752689}; |
Metal Binding | METAL 81; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 143; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 143; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 179; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 201; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 383; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550 |
Rhea ID | |
Cross Reference Brenda |