| IED ID | IndEnz0002005848 |
| Enzyme Type ID | protease005848 |
| Protein Name |
Carboxypeptidase B CPBHz EC 3.4.17.2 |
| Gene Name | CPB |
| Organism | Helicoverpa zea (Corn earworm moth) (Heliothis zea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Noctuoidea Noctuidae (owlet moths) Heliothinae Helicoverpa Helicoverpa zea (Corn earworm moth) (Heliothis zea) |
| Enzyme Sequence | MKFLLVLALCAVVYAKHEAYIGWKSYYVGVATDAQAKALEPLIQKYELDFLSHPTKSREGVVLVKPQHQAGFVQDIEAGGITYRIHADDVKRQLEFDDQLIEMQRMSSFTRTAGRQLPYDNYQELEVIDEYLDYIGEKYPDVATVVNAAESFEGRPIKYIKISTTNFEDENKPVIFIDGGIHAREWISPPSVTWAIHKLVEDVTENDLLEKFDWILLPVVNPDGYKYTFTNERFWRKTRSTNNNPLSQICRGADGNRNFDFVWNSIGTSNSPCSDIYAGTSAFSEVETRVVRDILHEHLARMALYLTMHSFGSMILYPWGHDGSLSQNALGLHTVGVAMASVIQSNALPNFPPYTVGNSALVIGYYIAGSSEDYAHSIGVPLSYTYELPGLSSGWDGFHLPPQYIEQVCRETWEGIVVGARRAGDLFRK |
| Enzyme Length | 429 |
| Uniprot Accession Number | Q3T905 |
| Absorption | |
| Active Site | ACT_SITE 387; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | ACTIVITY REGULATION: Highly resistant to inhibition by potato carboxypeptidase inhibitor (PCI). Moderately inhibited by leech carboxypeptidase inhibitor (LCI) and tick carboxypeptidase inhibitor (TCI). {ECO:0000269|PubMed:16260742}. |
| Binding Site | BINDING 236; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 365; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:16260742}; |
| DNA Binding | |
| EC Number | 3.4.17.2 |
| Enzyme Function | FUNCTION: Metalloprotease which cleaves a single amino acid from the C-terminal end of polypeptide chains. Shows a strong preference for peptides with a terminal lysine residue. {ECO:0000269|PubMed:16260742}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Binding site (2); Chain (1); Disulfide bond (1); Helix (14); Metal binding (3); Region (3); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2C1C; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,393 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 mM for benzoyl-glycyl-lysine (Bz-Gly-Lys) {ECO:0000269|PubMed:16260742}; KM=0.061 mM for N-(4-furylacryloyl)-Ala-Lys (FAAK) {ECO:0000269|PubMed:16260742}; Note=kcat is 45.7 sec(-1) for benzoyl-glycyl-lysine (Bz-Gly-Lys). kcat is 15.3 sec(-1) for N-(4-furylacryloyl)-Ala-Lys (FAAK). {ECO:0000269|PubMed:16260742}; |
| Metal Binding | METAL 182; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16260742, ECO:0007744|PDB:2C1C"; METAL 185; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16260742, ECO:0007744|PDB:2C1C"; METAL 309; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16260742, ECO:0007744|PDB:2C1C" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.2; |