| IED ID | IndEnz0002016763 |
| Enzyme Type ID | protease016763 |
| Protein Name |
Aminopeptidase N EC 3.4.11.2 Alanine aminopeptidase Lysyl aminopeptidase Lys-AP |
| Gene Name | pepN |
| Organism | Lactobacillus delbrueckii subsp. lactis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus delbrueckii Lactobacillus delbrueckii subsp. lactis |
| Enzyme Sequence | MAVKRFYETFHPDHYDLYIDVDRAARSFSGTSTIHGEIQEETVLVHQKYMTISKVTVDGKEVPFTFGDDFEGIKIEAGKTGEAVIAIDYSAPLTDTMMGIYPSYYQVDGVKKELIGTQFETTFAREAFPCVDEPEAKATFSLALKFDEHEGETVLANMPEDRVENGVHYFKETVRMSSYLVAFAFGEMRSLTTHTKSGVLIGVYSTQAHTEKELTFSLDIAKRAIEFYEDFYQTPYPLPQSLQLALPDFSAGAMENWGLVTYREAYLLLDPDNTTLEMKKLVATVVTHELAHQWFGDLVTMEWWDNLWLNESFANMMEYLSVDHLEPNWHIWEMFQTSEAAAALTRDATDGVQSVHVEVNDPAEIDALFDGAIVYAKGSRMLVMVRSLLGDEALRKGLKRYFDKHKFGNAAGDDLWDALSTATDLNIGEIMHTWLDQPGYPVVNAFVEDGHLKLTQKQFFIGEGKEVGRKWEIPLNANFKAPKIMSDVELDLGDYQALRAEAGHALRLNVGNNSHFIVKYDQTLMDDIMKEAKDLDPVSQLQLLQDLRLLAEGKQASYADVVPVLELFKNSESHIVNDALYTTADKLRQFAPAGSEADKNLRALYNDLSKDQVARLGWLPKAGESDEDIQTRPYVLSASLYGRNADSEKQAHEIYVEYADKLAELSADIRPYVLINEVENYGSSELTDKLIGLYQATSDPSFKMDLEAAIVKSKDEGELKKIVSWFKNAEIVKPQDLRGWFSGVLSNPAGEQLAWDWIRDEWAWLEKTVGGDMEFATFITVISRVFKTKERYDEYNAFFTDKESNMLLNREIKMDRKVIANRVDLIASEQADVNAAVAAALQK |
| Enzyme Length | 843 |
| Uniprot Accession Number | P37896 |
| Absorption | |
| Active Site | ACT_SITE 289; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 120; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | FUNCTION: Aminopeptidase with broad substrate specificity to several peptides. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 54-55 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Initiator methionine (1); Metal binding (3); Region (1); Site (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Note=It may be secreted through an unknown mechanism. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 95,348 |
| Kinetics | |
| Metal Binding | METAL 288; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 292; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 311; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |