| IED ID | IndEnz0002000431 |
| Enzyme Type ID | protease000431 |
| Protein Name |
Carboxypeptidase 1 EC 3.4.16.- Carboxypeptidase I CPD-I Fragment |
| Gene Name | |
| Organism | Aspergillus niger |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger |
| Enzyme Sequence | LTNKTARFLVNGTSIPEVDFDVGE |
| Enzyme Length | 24 |
| Uniprot Accession Number | P55749 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by DFP. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.16.- |
| Enzyme Function | FUNCTION: Removes acidic, neutral and basic amino acids as well as proline from the C-terminal position. Digests preferentially peptides containing a hydrophobic residue in P1' position, as well as arginine, lysine or phenylalanine in P1 position of ester substrate. Catalyzes also peptide synthesis. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4. Unstable above pH 8.; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (2); Non-terminal residue (1); Sequence uncertainty (2) |
| Keywords | Carboxypeptidase;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains both N- and O-linked sugar chains. The N-linked oligosaccharides are unique structures of Man(10)GlcNAc(2) and Man(11)GlcNAc(2). Deglycosylation does neither affect catalytic activity, pH, thermal stability, or resistance to proteolysis of the enzyme. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,623 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |