| IED ID | IndEnz0002005895 |
| Enzyme Type ID | protease005895 |
| Protein Name |
Carboxypeptidase O EC 3.4.17.- |
| Gene Name | cpo |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQEAYEGAMSIINYVHDKNFKNTAITVTATLWTTLMALWISTSHVF |
| Enzyme Length | 363 |
| Uniprot Accession Number | B8JLQ9 |
| Absorption | |
| Active Site | ACT_SITE 298; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by potato carboxypeptidase inhibitor, and the chelating agents EDTA and 1,10-phenanthroline. Also inhibited by compounds with multiple carboxylic acid groups such as citrate and succinate, and to a lesser exent the amino acids aspartate and glutamate. Not significantly inhibited by benzylsuccinic acid. {ECO:0000269|PubMed:21921028}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. {ECO:0000269|PubMed:21921028}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:21921028}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (4); Lipidation (1); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Cell membrane;Direct protein sequencing;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8IVL8}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:21921028}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:21921028 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,964 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=346 uM for 3-(2-furyl)acryloyl-Glu-Glu (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=324 uM for 3-(2-furyl)acryloyl-Phe-Phe (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=794 uM for 3-(2-furyl)acryloyl-Phe-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=743 uM for 3-(2-furyl)acryloyl-Lys-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; |
| Metal Binding | METAL 93; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 96; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 224; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda |