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 |