Detail Information for IndEnz0002016766
IED ID IndEnz0002016766
Enzyme Type ID protease016766
Protein Name Aminopeptidase N
EC 3.4.11.2
Alanine aminopeptidase
Lysyl aminopeptidase
Lys-AP
Gene Name pepN lap llmg_0319
Organism Lactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Lactococcus (lactic streptococci) Lactococcus lactis subsp. cremoris (Streptococcus cremoris) Lactococcus cremoris subsp. cremoris Lactococcus lactis subsp. cremoris (strain MG1363)
Enzyme Sequence MAVKRLIETFVPENYKIFLDIDRKTKKIKGQVAITGEAKDTVVSFHTKGLHFNKVRAFSVDTNFIENEEDEEIVVKIGETGRVTVSFEYEAELTDNMMGIYPSYYEVNGEKKMLIGTQFESHFARQAFPSIDEPEAKATFDLSVKFDEEEGDIIVSNMPELLNINGIHVFERTVKMSSYLLAFVFGELQYKKGKTKSGVEVGAFATKAHSQAALDFPLDIAIRSIEFYEDYYQTPYPLPHSWHIALPDFSAGAMENWGCITYREVCMLVDPENATIQSKQYVATVIAHELAHQWFGDLVTMQWWDDLWLNESFANNMEYVCMDALEPSWNVWESFSISEANMALNRDATDGVQSVHVEVTHPDEIGTLFDPAIVYAKGSRLMVMLRKWLGDEDFAAGLALYFKRHQYGNTVGDNLWDALAEVSGKDVAAFMHSWVNQPGYPVVTAEVVDDTLILSQKQFFVGEGVDKGRLWNVPLNTNWTGLPDLLSSEKVEIPGFAALKTKNNGKALFLNDANMAHYIIDYKGALLTDLLSEVESLENVTKFQILQDRKLLAKAGVISYADVVNILPSFTNEESYLVNTGLSQLISELELFVDEDSETEKAFQSLVGKLFAKNYARLGWDKVAGESAGDESLRGIVLSKTLYSENADAKTKASQIFAAHKENLASIPADIRPIVLNNEIKTTNSAELVKTYRETYIKTSLQEFKRELEGAVALIKDEKVIAELLESFKNADIVKPQDIAFSWFYLLRNDFSQDAAWAWEKANWAFLEEKLGGDMSYDKFVIYPGNTFKTADKLAEYKAFFEPKLENQGLKRSIEMAIKQITARVALIDSQKAAVDKAITDIAEKL
Enzyme Length 846
Uniprot Accession Number A2RI32
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.
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. 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 95,369
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