Detail Information for IndEnz0002019095
IED ID IndEnz0002019095
Enzyme Type ID protease019095
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 Z5872 ECs5237
Organism Escherichia coli O157:H7
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7
Enzyme Sequence MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFNGEE
Enzyme Length 503
Uniprot Accession Number P68768
Absorption
Active Site ACT_SITE 282; /evidence=ECO:0000255; ACT_SITE 356; /evidence=ECO:0000255
Activity Regulation ACTIVITY REGULATION: Inhibited by zinc and EDTA. {ECO:0000250}.
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: Presumably involved in the processing and regular turnover of intracellular proteins. 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 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 54,880
Kinetics
Metal Binding METAL 270; /note=Manganese 2; /evidence=ECO:0000250; METAL 275; /note=Manganese 1; /evidence=ECO:0000250; METAL 275; /note=Manganese 2; /evidence=ECO:0000250; METAL 293; /note=Manganese 2; /evidence=ECO:0000250; METAL 352; /note=Manganese 1; /evidence=ECO:0000250; METAL 354; /note=Manganese 1; /evidence=ECO:0000250; METAL 354; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda