| IED ID | IndEnz0002004474 |
| Enzyme Type ID | protease004474 |
| Protein Name |
Zinc carboxypeptidase EC 3.4.17.18 |
| Gene Name | |
| Organism | Saccharothrix mutabilis subsp. capreolus (Streptomyces capreolus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Pseudonocardiales Pseudonocardiaceae Saccharothrix Saccharothrix mutabilis Saccharothrix mutabilis subsp. capreolus (Streptomyces capreolus) |
| Enzyme Sequence | MSPKRRRLMAAALGACVALVLPLHAGSAQPSTAKTPERTVFEVTASTPEARTRVARTGVDVLGQDGDKLTVVAEPRQQWALRATGLRVENLGDYDAQLQALGKVDFTDPQVGTQDFPSGYTGYHNFQETVTELNQTVTDHPNLVRLSSVGKSYQGRDLWMLKLSDNPAVDENEPEVLFTCNMHAREHLTVEMCLRIIKQYTDGYATNPTIKNLVDSREIWIIPMVNPDGVEYDIATGSFRSWRKNRQPNSTAVGTDPNRNWGYQWGCCGGSSSSGSSETTAARRRSPPRRSPHPHFVNTRVVGGVQQIKTHIDWHTYSELILWPYGYTYNDTAPGLDAQQASAFSTLGRRMASLNGTRRQQSSDLYITDGTINDWLWGVHKIWSYTFEMYPKSSSPGFYPRDTVIATQTQRNDSAVELFLSYSDCVPRIIGRTC |
| Enzyme Length | 434 |
| Uniprot Accession Number | P39041 |
| Absorption | |
| Active Site | ACT_SITE 388; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Releases a C-terminal residue, which may be hydrophobic or positively charged.; EC=3.4.17.18; Evidence={ECO:0000250|UniProtKB:P18143}; |
| DNA Binding | |
| EC Number | 3.4.17.18 |
| Enzyme Function | FUNCTION: Carboxypeptidase that possesses the specificities of both mammalian Cpase A and B. Thus shows broad substrate specificity, being able to cleave Cbz-Gly-Leu, Cbz-Gly-Val, Cbz-Gly-Phe, Cbz-Gly-Lys and Bz-Gly-Arg in vitro. {ECO:0000250|UniProtKB:P18143}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,477 |
| Kinetics | |
| Metal Binding | METAL 183; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 186; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 315; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.18; |