| IED ID | IndEnz0002019091 |
| Enzyme Type ID | protease019091 |
| Protein Name |
Cytosol aminopeptidase EC 3.4.11.1 Aminopeptidase A/I Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA carP xerB b4260 JW4217 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE |
| Enzyme Length | 503 |
| Uniprot Accession Number | P68767 |
| Absorption | |
| Active Site | ACT_SITE 282; /evidence=ECO:0000255; ACT_SITE 356; /evidence=ECO:0000255 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by zinc and EDTA. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Probably involved in the processing and regular turnover of intracellular proteins (PubMed:20067529). Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place (PubMed:8057849). {ECO:0000269|PubMed:8057849, ECO:0000305|PubMed:20067529}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (20); Chain (1); Helix (22); Metal binding (7); Mutagenesis (1); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1GYT; |
| Mapped Pubmed ID | 14741201; 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,880 |
| Kinetics | |
| Metal Binding | METAL 270; /note=Manganese 2; /evidence=ECO:0000305; METAL 275; /note=Manganese 1; /evidence=ECO:0000305; METAL 275; /note=Manganese 2; /evidence=ECO:0000305; METAL 293; /note=Manganese 2; /evidence=ECO:0000305; METAL 352; /note=Manganese 1; /evidence=ECO:0000305; METAL 354; /note=Manganese 1; /evidence=ECO:0000305; METAL 354; /note=Manganese 2; /evidence=ECO:0000305 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.1; |