| IED ID | IndEnz0002002068 |
| Enzyme Type ID | protease002068 |
| Protein Name |
Leucine aminopeptidase 2 EC 3.4.11.- Leucyl aminopeptidase 2 LAP2 |
| Gene Name | LAP2 |
| Organism | Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum) |
| Enzyme Sequence | MKSQLLSLAVAVTTISQGVVGQEPFGWPFKPMVTQDDLQNKIKLKDIMAGVEKLQSFSDAHPEKNRVFGGNGHKDTVEWIYNEIKATGYYDVKKQEQVHLWSHAEAALNANGKDLKASAMSYSPPASKIMAELVVAKNNGCNATDYPANTQGKIVLVERGVCSFGEKSAQAGDAKAAGAIVYNNVPGSLAGTLGGLDKRHVPTAGLSQEDGKNLATLVASGKIDVTMNVISLFENRTTWNVIAETKGGDHNNVIMLGAHSDSVDAGPGINDNGSGSIGIMTVAKALTNFKLNNAVRFAWWTAEEFGLLGSTFYVNSLDDRELHKVKLYLNFDMIGSPNFANQIYDGDGSAYNMTGPAGSAEIEYLFEKFFDDQGIPHQPTAFTGRSDYSAFIKRNVPAGGLFTGAEVVKTPEQVKLFGGEAGVAYDKNYHRKGDTVANINKGAIFLNTRAIAYAIAEYARSLKGFPTRPKTGKRDVNPQYSKMPGGGCGHHTVFM |
| Enzyme Length | 495 |
| Uniprot Accession Number | Q5QHG6 |
| Absorption | |
| Active Site | ACT_SITE 303; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by EDTA, o-phenanthroline, bestatin and amastatin. {ECO:0000269|PubMed:15632434}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Extracellular aminopeptidase that releases a wide variety of amino acids from natural peptides and contributes to pathogenicity. {ECO:0000269|PubMed:15632434}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperatures are ranging from 40 to 50 degrees Celsius. {ECO:0000269|PubMed:15632434}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:15632434}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (4); Metal binding (6); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Virulence;Zinc |
| Interact With | |
| Induction | INDUCTION: Expression is strongly increased during growth on protein-rich medium. Expression levels are the same whether keratin is present or not in the protein-rich medium. {ECO:0000269|PubMed:19098130}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15632434}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,309 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 271; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 271; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 304; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 332; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 430; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda |