| IED ID | IndEnz0002001707 |
| Enzyme Type ID | protease001707 |
| Protein Name |
Prolyl tri/tetrapeptidyl aminopeptidase PTP-SM EC 3.4.11.- Tripeptidyl aminopeptidase SM-TAP |
| Gene Name | ptp |
| Organism | Streptomyces mobaraensis (Streptoverticillium mobaraense) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces mobaraensis (Streptoverticillium mobaraense) |
| Enzyme Sequence | MRKALRSLLAASMLIGAIGAGSATAEAASITAPQADIKDRILKIPGMKFVEEKPYQGYRYLVMTYRQPVDHRNPGKGTFEQRFTLLHKDTDRPTVFFTSGYNVSTNPSRSEPTRIVDGNQVSMEYRFFTPSRPQPADWSKLDIWQAASDQHRLYQALKPVYGKNWLATGGSKGGMTATYFRRFYPNDMNGTVAYVAPNDVNDKEDSAYDKFFQNVGDKACRTQLNSVQREALVRRDEIVARYEKWAKENGKTFKVVGSADKAYENVVLDLVWSFWQYHLQSDCASVPATKASTDELYKFIDDISGFDGYTDQGLERFTPYYYQAGTQLGAPTVKNPHLKGVLRYPGINQPRSYVPRDIPMTFRPGAMADVDRWVREDSRNMLFVYGQNDPWSGEPFRLGKGAAARHDYRFYAPGGNHGSNIAQLVADERAKATAEVLKWAGVAPQAVQKDEKAAKPLAPFDAKLDRVKNDKQSALRP |
| Enzyme Length | 477 |
| Uniprot Accession Number | P83615 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by the serine protease inhibitor phenylmethylsulfonyl fluoride. Partially inhibited by the serine protease inhibitor Pefabloc. Not inhibited by cysteine proteinase-specific or metalloproteinase-specific inhibitors. Not inhibited by prolinal or its derivatives. EDTA and EGTA both partially inhibit this enzyme (PubMed:14519127). EDTA has no effect on activity (PubMed:15598885). {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Has proline-specific tripeptidyl aminopeptidase and tetrapeptidyl aminopeptidase activity. Activity is highest against tripeptides containing an Ala-Pro motif. Involved in the final processing of transglutaminase, by removing either the tetrapeptide Phe-Arg-Ala-Pro left after TAMEP or SAM-P45 hydrolysis, or the tripeptide Arg-Ala-Pro left after SGMP II hydrolysis in a single step. {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5 (PubMed:14519127). Optimum pH is 6.0-6.5 (PubMed:15598885). Active between pH 4.3 and 8.3. Stable after 12 hours incubation from pH 4.0 to 9.0. {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Hydrolase;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cell surface. Note=Secreted (PubMed:14519127). Cell surface (PubMed:15598885). {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,702 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.072 mM for Gly-Ala-Pro-BNA {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}; KM=0.26 mM for Gly-Ala-Gly-Pro-BNA {ECO:0000269|PubMed:14519127, ECO:0000269|PubMed:15598885}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |