Detail Information for IndEnz0002014535
IED ID IndEnz0002014535
Enzyme Type ID protease014535
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA PM0195
Organism Pasteurella multocida (strain Pm70)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Pasteurella Pasteurella multocida Pasteurella multocida subsp. multocida Pasteurella multocida (strain Pm70)
Enzyme Sequence MEYRVKSTALLDIKSNIIIGLYENGELSPSAQKIDEISQGYLSKLIQSGEIKGKLGQVLVLRHVPNYSAERVFVVGAGKKGEINEKQFKQLIQDTINAVKATSAKEVISYLSDIKIKDRDLYWNIRFSVETLETSIYQFEQFKSKKSEQDVALTDVIFSAEGDVAQQAVNHAKAIALGVRAAKDVANCPPNVCNPVYLAEQANALATRSDLIKTTVLGEKDMADLGMNAYLAVSQGSVNEAQLSLIEYRNHPNPDAKPIVLVGKGLTFDAGGISLKPAEGMDEMKYDMGGAASVYGVMNAIAELKLPLNVIGVLAGCENLPDGNAYRPGDILTTMKGLTVEVLNTDAEGRLVLCDTLTYVERFEPELVIDVATLTGACVVALGAHNSGLISTDDKLAKDLELAAAQSTDKAWRLPLGEEYQEQLKSNFADLANIGGRWGGAITAGAFLSNFTDKYRWAHLDIAGTAWLQGANKGATGRPVPLLVQFLINQATGK
Enzyme Length 494
Uniprot Accession Number P57823
Absorption
Active Site ACT_SITE 276; /evidence=ECO:0000255; ACT_SITE 350; /evidence=ECO:0000255
Activity Regulation
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 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 53,300
Kinetics
Metal Binding METAL 264; /note=Manganese 2; /evidence=ECO:0000250; METAL 269; /note=Manganese 1; /evidence=ECO:0000250; METAL 269; /note=Manganese 2; /evidence=ECO:0000250; METAL 287; /note=Manganese 2; /evidence=ECO:0000250; METAL 346; /note=Manganese 1; /evidence=ECO:0000250; METAL 348; /note=Manganese 1; /evidence=ECO:0000250; METAL 348; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda