| IED ID | IndEnz0002007652 |
| Enzyme Type ID | protease007652 |
| Protein Name |
Aminopeptidase EC 3.4.11.- Fragment |
| Gene Name | |
| Organism | Capnocytophaga gingivalis |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Flavobacteriaceae Capnocytophaga Capnocytophaga gingivalis Capnocytophaga gingivalis |
| Enzyme Sequence | DVNMLWYVXR |
| Enzyme Length | 10 |
| Uniprot Accession Number | P80474 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Aminopeptidase which hydrolyzes substrates with free N-terminal amino acid residues but not N-terminal blocked ones. May be important in the nutrition and pathogenesis of the organism in the human oral cavity. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (2) |
| Keywords | Aminopeptidase;Calcium;Direct protein sequencing;Hydrolase;Magnesium;Protease |
| 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 | 1,307 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |