| IED ID | IndEnz0002000600 |
| Enzyme Type ID | protease000600 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase L9PepTR Tripeptide aminopeptidase |
| Gene Name | pepT |
| Organism | Lactococcus lactis subsp. lactis (Streptococcus lactis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis Lactococcus lactis subsp. lactis (Streptococcus lactis) |
| Enzyme Sequence | MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIKLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNTMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIVPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVVK |
| Enzyme Length | 413 |
| Uniprot Accession Number | Q76HM5 |
| 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 | ACTIVITY REGULATION: Activity is strongly inhibited in vitro by chelating agents such as EDTA and 1,10-phenanthroline as do the reducing agent dithiothreitol and the oxidizing agent N-bromosuccinimid. Phenylmethylsulfonyl fluoride, a serine protease inhibitor has no influence on the enzyme activity. On the other hand, bestatin, an aminopeptidase inhibitor strongly inhibits the enzyme activity and leupeptin, a modified tripeptide, slightly inhibits it. {ECO:0000269|PubMed:16233215}. |
| 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, ECO:0000269|PubMed:16233215}; |
| 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, ECO:0000269|PubMed:16233215}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 44 degrees Celsius. The enzyme is stable up to 50 degrees Celsius. {ECO:0000269|PubMed:15752689, ECO:0000269|PubMed:16233215}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 8. The enzyme is stable in a pH range of 9-10. {ECO:0000269|PubMed:15752689, ECO:0000269|PubMed:16233215}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cobalt;Cytoplasm;Direct protein sequencing;Hydrolase;Manganese;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 | 45,972 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.147 mM for AAA tripeptide {ECO:0000269|PubMed:15752689}; KM=0.390 mM for GAA tripeptide {ECO:0000269|PubMed:15752689}; KM=0.598 mM for AGA tripeptide {ECO:0000269|PubMed:15752689}; KM=1.29 mM for AAG tripeptide {ECO:0000269|PubMed:15752689}; KM=0.770 mM for GGA tripeptide {ECO:0000269|PubMed:15752689}; KM=1.57 mM for AGG tripeptide {ECO:0000269|PubMed:15752689}; KM=4.52 mM for GAG tripeptide {ECO:0000269|PubMed:15752689}; KM=12.0 mM for GGG tripeptide {ECO:0000269|PubMed:15752689}; KM=1.77 mM for YGG tripeptide {ECO:0000269|PubMed:15752689}; KM=2.44 mM for LGG tripeptide {ECO:0000269|PubMed:15752689}; KM=3.54 mM for FGG tripeptide {ECO:0000269|PubMed:15752689}; KM=6.49 mM for SGG tripeptide {ECO:0000269|PubMed:15752689}; KM=10.6 mM for AibGG tripeptide {ECO:0000269|PubMed:15752689}; Note=kcat is 163 sec(-1) with AAA tripeptide as substrate. kcat is 616 sec(-1) with GAA tripeptide as substrate. kcat is 713 sec(-1) with AGA tripeptide as substrate. kcat is 730 sec(-1) with AAG tripeptide as substrate. kcat is 507 sec(-1) with GGA tripeptide as substrate. kcat is 573 sec(-1) with AGG tripeptide as substrate. kcat is 1093 sec(-1) with GAG tripeptide as substrate. kcat is 502 sec(-1) with GGG tripeptide as substrate. kcat is 292 sec(-1) with YGG tripeptide as substrate. kcat is 197 sec(-1) with LGG tripeptide as substrate. kcat is 262 sec(-1) with FGG tripeptide as substrate. kcat is 270 sec(-1) with SGG tripeptide as substrate. kcat is 31.2 sec(-1) with AibGG tripeptide as substrate. kcat is 453 sec(-1) with GGF tripeptide as substrate. kcat is 806 sec(-1) with GAY 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 |