Detail Information for IndEnz0002018787
IED ID IndEnz0002018787
Enzyme Type ID protease018787
Protein Name Cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA
Organism Pseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas putida group Pseudomonas putida (Arthrobacter siderocapsulatus)
Enzyme Sequence MELVVKSVAAASVKTATLVIPVGENRKLGAVAKAVDLASEGAISAVLKRGDLAGKPGQTLLLQNLQGLKAERVLLVGSGKDEALGDRTWRKLVASVAGVLKGLNGADAVLALDDVAVNNRDAHYGKYRLLAETLLDGEYVFDRFKSQKVEPRALKKVTLLADKAGQAEVERAVKHASAIATGMAFTRDLGNLPPNLCHPSFLAEQAKELGKAHKALKVEVLDEKKIKDLGMGAFYAVGQGSDQPPRLIVLNYQGGKKADKPFVLVGKGITFDTGGISLKPGAGMDEMKYDMCGAASVFGTLRAVLELQLPVNLVCLLACAENMPSGGATRPGDIVTTMSGQTVEILNTDAEGRLVLCDTLTYAERFKPQAVIDIATLTGACIVALGSHTTGLMGNNDDLVGQLLDAGKRADDRAWQLPLFDEYQEQLDSPFADMGNIGGPKAGTITAGCFLSRFAKAYNWAHMDIAGTAWISGGKDKGATGRPVPLLTQYLLDRAGA
Enzyme Length 497
Uniprot Accession Number O86436
Absorption
Active Site ACT_SITE 279; /evidence=ECO:0000255; ACT_SITE 353; /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); Beta strand (21); Chain (1); Helix (21); Metal binding (7); Turn (5)
Keywords 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 3H8E; 3H8F; 3H8G;
Mapped Pubmed ID 20359484;
Motif
Gene Encoded By
Mass 52,469
Kinetics
Metal Binding METAL 267; /note=Manganese 2; /evidence=ECO:0000250; METAL 272; /note=Manganese 1; /evidence=ECO:0000250; METAL 272; /note=Manganese 2; /evidence=ECO:0000250; METAL 290; /note=Manganese 2; /evidence=ECO:0000250; METAL 349; /note=Manganese 1; /evidence=ECO:0000250; METAL 351; /note=Manganese 1; /evidence=ECO:0000250; METAL 351; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.11.10;