Detail Information for IndEnz0002014537
IED ID IndEnz0002014537
Enzyme Type ID protease014537
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA LA_3441
Organism Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Leptospirales Leptospiraceae Leptospira Leptospira interrogans Leptospira interrogans serovar Lai Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Enzyme Sequence MKLDKNKIQISIGKNPSKTFYKLQLLLKDHFPENLKTKFSFQTASGIFTGENGQIFTDEVEKIIYLGLGETSKIKIRGVAQHFFQFGEKLKKWEGVGLEIHLPKVLTNSLSADLVVYQIVNSLEQGVYAINVLAKEYKENSKKIGNVSFILQDAAKLKEAEKGLKRGKIVSRYINGVRHIAHLPANHFTPEEFVSRSKEIAKDNGLKITVFDEPQLKKEKMGGILSVCEGSDKKAKMILLEYTPVKPITKKKLAIIGKGLTFDSGGISIKPAQDMHEMKYDMCGAATAIHAIGAIAELGLGVPVIAAIGVAENMPDAAAIKPGDVYTAYNGITVEVQNTDAEGRLVLGDVLSYVGKKFKPDYMLDLATLTGAIIISLGHEAAGVMSNSDVLTNLLKEASISSDERIWEMPLWEEYSEDLKSDIADIRNVAGRAGGSLSAAKFLERFVEPGIAWAHIDIAGTAWRKKTSGTQIGNGPTGYGVRLLVDLVEKIGKKK
Enzyme Length 495
Uniprot Accession Number Q8F0Q1
Absorption
Active Site ACT_SITE 270; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 344; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
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. {ECO:0000255|HAMAP-Rule:MF_00181}.
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:0000255|HAMAP-Rule:MF_00181}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 54,077
Kinetics
Metal Binding METAL 258; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 263; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 263; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 281; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 340; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 342; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 342; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda