| IED ID | IndEnz0002005980 |
| Enzyme Type ID | protease005980 |
| Protein Name |
Carboxypeptidase O CPO EC 3.4.17.- |
| Gene Name | CPO |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKPLLETLYLLGMLVPGGLGYDRSLAQHRQEIVDKSVSPWSLETYSYNIYHPMGEIYEWMREISEKYKEVVTQHFLGVTYETHPMYYLKISQPSGNPKKIIWMDCGIHAREWIAPAFCQWFVKEILQNHKDNSSIRKLLRNLDFYVLPVLNIDGYIYTWTTDRLWRKSRSPHNNGTCFGTDLNRNFNASWCSIGASRNCQDQTFCGTGPVSEPETKAVASFIESKKDDILCFLTMHSYGQLILTPYGYTKNKSSNHPEMIQVGQKAANALKAKYGTNYRVGSSADILYASSGSSRDWARDIGIPFSYTFELRDSGTYGFVLPEAQIQPTCEETMEAVLSVLDDVYAKHWHSDSAGRVTSATMLLGLLVSCMSLL |
| Enzyme Length | 374 |
| Uniprot Accession Number | Q8IVL8 |
| Absorption | |
| Active Site | ACT_SITE 310; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00730 |
| 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 | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Glycosylation (4); Helix (12); Lipidation (1); Metal binding (3); Natural variant (3); Propeptide (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;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:0000269|PubMed:21921028}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21921028}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:21921028}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:21921028 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5MRV; |
| Mapped Pubmed ID | 29636417; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,529 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=325 uM for 3-(2-furyl)acryloyl-Glu-Glu (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=284 uM for 3-(2-furyl)acryloyl-Phe-Phe (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=549 uM for 3-(2-furyl)acryloyl-Phe-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=614 uM for 3-(2-furyl)acryloyl-Lys-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; |
| Metal Binding | METAL 108; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 111; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 236; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda |