| IED ID | IndEnz0002005142 |
| Enzyme Type ID | protease005142 |
| Protein Name |
Carboxypeptidase CP EC 3.4.17.- Fragments |
| Gene Name | |
| Organism | Sabellastarte magnifica (Feather duster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Polychaeta (polychaetes) Sedentaria Canalipalpata Sabellida Sabellidae Sabellastarte Sabellastarte magnifica (Feather duster) |
| Enzyme Sequence | AFDLNDFNTLEDTYDQMNVFQLSEAGLTHEGRDMKSWIDSLTHCRSHLDEDVFMFKRNEPDSGSACVGTDLNRSSNNPCSDTYGGSGPASALETRHSYSQQYEDELNQRQRYEPSGTTVNNLLNKDAGSIYSYTPELR |
| Enzyme Length | 138 |
| Uniprot Accession Number | P86516 |
| Absorption | |
| Active Site | ACT_SITE 136; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by the A-type carboxypeptidase inhibitor benzylsuccinic acid. Inhibited by the leech carboxypeptidase inhibitor and the potato carboxydase inhibitor. Inhibited by the chelating agent 1,10-phenanthroline. Partial inhibition by preincubation with the chelating agent EDTA is reversed by addition of Zn(2+). Not inhibited by the cysteine protease inhibitors L-carboxy-trans-2,3-epoxypropyl-leycylamido (4-guanidino) butane, E-64 and cystatin, the aspartic protease inhibitor pepstatin, or the serine protease inhibitors Pefabloc, soybean trypsin-chymotrypsin inhibitor, soybean trypsin inhibitor and aprotinin. {ECO:0000269|PubMed:19694804}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase that catalyzes the release of hydrophobic and acidic C-terminal amino acids. {ECO:0000269|PubMed:19694804}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5 with AAFP as substrate. {ECO:0000269|PubMed:19694804}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Metal binding (2); Non-adjacent residues (9); Non-terminal residue (1); Region (4) |
| Keywords | Carboxypeptidase;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00732}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,590 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 mM for N-(4-methoxyphenylazoformyl)-L-phenyl-alanine (AAFP) {ECO:0000269|PubMed:19694804}; KM=0.36 mM for hippuryl-Phe {ECO:0000269|PubMed:19694804}; KM=0.14 mM for N-(3-[2-furyl]acryloyl)-Phe-Phe (FAPP) {ECO:0000269|PubMed:19694804}; |
| Metal Binding | METAL 43; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15086; METAL 96; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15086 |
| Rhea ID | |
| Cross Reference Brenda |