Detail Information for IndEnz0002014029
IED ID IndEnz0002014029
Enzyme Type ID protease014029
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA yuiE BSU32050
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MFYAVQQSEHTETLVVGLFQKSQLTGKALEIDEMLEGHLTQLLKEGDVSAKPNQVSKVFPPSSAGMKRIYFVGLGREANYSFEQAKERFAHVFQAIHKDRKQETAVLLDTFISEDVPPADAAHALAESCLLASYEVQDYKHKSNEPDKQIEAVYVVTDEDTQEVQAGLRVGQAYGQGTNSARTLVNMPGNMLTATDLASYAEELAAKYDFECEILEKSEMEELGMGGILAVNQGSTEPPKMIVLKYQGKKEWEDVVGLVGKGITFDTGGYSIKTKSGIVGMKSDMGGAAAVLGAMETIGELRPEQNVLCVIPSTDNMISGGAMKPDDVIVSLSGKTIEILNTDAEGRLVLADGITYAKQHGASVLVDVATLTGGVVVALGTETTGAMTNDQSFYQQVADAAQECGEAIWQLPITEKDKKRVKSSQMADLSNSPGREGHAIMAGTFLGEFAESTPWVHLDIAGTATANKATCFGPAGATGVMARTLATLAERFTLEEDKNE
Enzyme Length 500
Uniprot Accession Number O32106
Absorption
Active Site ACT_SITE 273; /evidence=ECO:0000255; ACT_SITE 347; /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 53,658
Kinetics
Metal Binding METAL 261; /note=Manganese 2; /evidence=ECO:0000250; METAL 266; /note=Manganese 1; /evidence=ECO:0000250; METAL 266; /note=Manganese 2; /evidence=ECO:0000250; METAL 284; /note=Manganese 2; /evidence=ECO:0000250; METAL 343; /note=Manganese 1; /evidence=ECO:0000250; METAL 345; /note=Manganese 1; /evidence=ECO:0000250; METAL 345; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.11.1;3.4.11.10;