| IED ID | IndEnz0002005083 |
| Enzyme Type ID | protease005083 |
| Protein Name |
M1 family aminopeptidase EC 3.4.11.- Pfa-M1 |
| Gene Name | |
| Organism | Plasmodium falciparum (isolate FcB1 / Columbia) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate FcB1 / Columbia) |
| Enzyme Sequence | MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL |
| Enzyme Length | 1085 |
| Uniprot Accession Number | O96935 |
| Absorption | |
| Active Site | ACT_SITE 497; /note=Proton acceptor; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline, EDTA and bestatin. Activity is not affected by phosphoramidin, PMSF, leupeptin, iodoacetamide or pepstatin. {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988}. |
| Binding Site | BINDING 319; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC. {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. Active from pH 5.8 to 8.6, with less than 20% of normal activity at pH 6.0. {ECO:0000269|PubMed:19196988}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (30); Binding site (1); Chain (1); Compositional bias (1); Helix (39); Metal binding (3); Region (2); Site (1); Turn (11) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. |
| Modified Residue | |
| Post Translational Modification | PTM: The 120 kDa precursor is cleaved in vitro into 96 kDa and 68 kDa forms. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (45) |
| Cross Reference PDB | 3EBG; 3EBH; 3EBI; 3Q43; 3Q44; 3T8V; 4J3B; 4K5L; 4K5M; 4K5N; 4K5O; 4K5P; 4R5T; 4R5V; 4R5X; 4X2U; 4ZW3; 4ZW5; 4ZW6; 4ZW7; 4ZW8; 4ZX3; 4ZX4; 4ZX5; 4ZX6; 5XM7; 5Y19; 5Y1H; 5Y1K; 5Y1Q; 5Y1R; 5Y1S; 5Y1T; 5Y1V; 5Y1W; 5Y1X; 5Y3I; 6EA1; 6EA2; 6EAA; 6EAB; 6EE3; 6EE4; 6EE6; 6EED; |
| Mapped Pubmed ID | 21844374; 23713488; 23897806; 25299353; 25645579; 26807544; 30537832; |
| Motif | |
| Gene Encoded By | |
| Mass | 126,062 |
| Kinetics | |
| Metal Binding | METAL 496; /note=Zinc; catalytic; METAL 500; /note=Zinc; catalytic; METAL 519; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.20; |