| IED ID | IndEnz0002004730 |
| Enzyme Type ID | protease004730 |
| Protein Name |
Thermostable carboxypeptidase 1 EC 3.4.17.19 Carboxypeptidase Taq |
| Gene Name | |
| Organism | Thermus aquaticus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Thermus Thermus aquaticus |
| Enzyme Sequence | MTPEAAYQNLLEFQRETAYLGSLGALAAWDQRTMIPRKGHGHRARQMAALARLLHERATDPRIGEWLEKVEGSSLVEDPLSDAAVNVRAWRRAYERARAIPERLAVELAQARSEGETAWEALRPRDDWQGFLPYLKRLFALAKEEAEILMAVGPDPLDPPYGELYDALLDGYEPGARARDLEPLFRELSSGLKGLLDRILGSGRRPDVGVLHRHYPKEAQRAFALELLQACGYDLEAGRLDPTAHPFEIAIGPGDVRITTRYYEDFFNAGIFGTLHEMGHALYEQGLPEAHWGTPRGEAASLGVHESQSRTWENLVGRSLGFWERFFPRAKEVFSSLADVRLEDFHFAVNAVEPSLIRVEADEVTYNLHILVRLELELALFRGELFLEDLPEAWREKYRAYLGVAPRDYKDGVMQDVHWSGGMFGYFPTYTLGNLYAAQFFAKAQEELGPLEPLFARGEFTPFLDWTRRKIHAEGSRFRPRALVERVTGSPPGAQAFLRYLEAKYGALYGF |
| Enzyme Length | 511 |
| Uniprot Accession Number | P42663 |
| Absorption | |
| Active Site | ACT_SITE 277; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:8862545 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by metal-chelating reagents. Strongly inhibited by 1 mM Zn(2+), slightly inhibited by 0.1 mM Zn(2+), not inhibited by 0.01 mM Zn(2+). Not inhibited by cobalt ions. {ECO:0000269|PubMed:1369078, ECO:0000269|PubMed:7765282}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity, except for -Pro.; EC=3.4.17.19; Evidence={ECO:0000269|PubMed:1369078, ECO:0000269|PubMed:7765282, ECO:0000269|PubMed:8862545}; |
| DNA Binding | |
| EC Number | 3.4.17.19 |
| Enzyme Function | FUNCTION: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro. {ECO:0000269|PubMed:1369078, ECO:0000269|PubMed:7765282}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:1369078}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:1369078}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Mutagenesis (8); Sequence conflict (1) |
| Keywords | Carboxypeptidase;Cobalt;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,954 |
| Kinetics | |
| Metal Binding | METAL 276; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:8862545"; METAL 280; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:8862545"; METAL 306; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:8862545" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.19; |