| IED ID | IndEnz0002016764 |
| Enzyme Type ID | protease016764 |
| Protein Name |
Aminopeptidase N EC 3.4.11.2 Alanine aminopeptidase Lysyl aminopeptidase Lys-AP |
| Gene Name | pepN lap |
| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Enzyme Sequence | MAVKRLIETFVPENYKIFLDIDRKTKKIKGQVAITGEAKDTVVAFHAKGLHFNKVRAFSVDTNFIENEEDEEIVVKIGETGRVTVSFEYEAELTDNMMGIYPSYYEVNGEKKMLIGTQFESHFARQAFPSIDEPEAKATFDLSVKFDEEEGDIIVSNMPELLNINGIHVFERTVKMSSYLLAFVFGELQYKKGKTKSGVEVGAFATKAHSQAALDFPLDIAIRSIEFYEDYYQTPYPLPHSWHIALPDFSSGAMENWGCITYREVCMLVDPENATIQSKQYVATVIAHELAHQWFGDLVTMQWWDDLWLNESFANNMEYVCMDALEPSWNVWESFSISEANMALNRDATDGVQSVHVEVTHPDEIGTLFDPAIVYAKGSRLMVMLRKWLGDEDFAAGLALYFKRHQYGNTVGDNLWDALAEVSGKDVAAFMHSWVNQPGYPVVTAEVVDDTLILSQKQFFVGEGVDKGRLWNVPLNTNWTGLPDLLSSEKVEIPGFAALKTKNNGKALFLNDANMAHYIIDYKGALLTDLLSEVESLENVTKFQILQDRKLLAKAGVISYADVVNILPSFTNEESYLVNTGLSQLISELELFVDEDSETEKAFQSLVGKLFAKNYARLGWDKVAGESAGDESLRGIVLSKTLYSENADAKTKASQIFATHKENLASIPADIRPIVLNNEIKTTNSAELVKTYRETYIKTSLQEFKRELEGAVALIKDEKVIAELLESFKNADIVKPQDIAFSWFYLLRNDFSQDAAWAWEKANWASLEEKLGGDMSYDKFVIYPGNTFKTADKLAEYKAFFEPKLENQGLKRSIEMAIKQITARVALIDSQKAAVDKAITDIAEKL |
| Enzyme Length | 846 |
| Uniprot Accession Number | P0C2T8 |
| 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. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| 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;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=It may be secreted through an unknown mechanism. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 95,309 |
| 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 |