| IED ID | IndEnz0002002325 |
| Enzyme Type ID | protease002325 |
| Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M Fragment |
| Gene Name | map |
| Organism | Klebsiella oxytoca |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Klebsiella Klebsiella oxytoca |
| Enzyme Sequence | TVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHNE |
| Enzyme Length | 43 |
| Uniprot Accession Number | P41392 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Aminopeptidase;Hydrolase;Metal-binding;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 | 4,826 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |