| IED ID | IndEnz0002016746 |
| Enzyme Type ID | protease016746 |
| Protein Name |
Cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP Leucyl aminopeptidase Proline aminopeptidase EC 3.4.11.5 Prolyl aminopeptidase |
| Gene Name | lap DDB_G0279793 |
| Organism | Dictyostelium discoideum (Slime mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
| Enzyme Sequence | MLKNIINKKNLFINNQQNIFQIIKRNKMTDSTVDNKGYIVGIYENEEFTPLGQQLNEKTNGHLLKSIKLSDTKGKVGDNLVLYNVTPEVSRVAIVGLGKKENNNSTTYEKNENTRKAIGSGVKALKSKNATHLTIDSNIGDAKQTAEGAFLSNFKFDFKTGTSGKTANSTNESIQVQLSPSPSSEECFKEGKILAESQNFARVLMETPANLLTPTNFVQHVSSQMKELIDSGKVEMIVREEQWVKDQKMGMFWGVAKGSDEPLKFLELHYRGASADGKDSIVYVGKGITFDSGGISIKPSANMGLMKGDMGGAATAVSAMFGVASLGLKVNLITITPLCENMPSGKATKPGDILTAANGKTVEVDNTDAEGRLILGDALHYACSFKPTHIIDIATLTGAIDVALGQHYAGCFTTTDSLWDQLNECGNISGERLWRMPLIPEYRKQMETSKVADLINSAGRSGGACCAAGFLKEFITADQSWSHLDIAGVMSSSEDGPYIRKGMTGKPTRTLIEFAKKNQQ |
| Enzyme Length | 520 |
| Uniprot Accession Number | Q5V9F0 |
| Absorption | |
| Active Site | ACT_SITE 298; /evidence=ECO:0000250; ACT_SITE 372; /evidence=ECO:0000250 |
| 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 N-terminal proline from a peptide.; EC=3.4.11.5; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.5 |
| 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;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc |
| 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 | 1033094; 22120990; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,410 |
| Kinetics | |
| Metal Binding | METAL 286; /note=Zinc 2; /evidence=ECO:0000250; METAL 291; /note=Zinc 1; /evidence=ECO:0000250; METAL 291; /note=Zinc 2; /evidence=ECO:0000250; METAL 309; /note=Zinc 2; /evidence=ECO:0000250; METAL 368; /note=Zinc 1; /evidence=ECO:0000250; METAL 370; /note=Zinc 1; /evidence=ECO:0000250; METAL 370; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |