IED ID | IndEnz0002015954 |
Enzyme Type ID | protease015954 |
Protein Name |
Leucine aminopeptidase 1 EC 3.4.11.- Leucyl aminopeptidase 1 LAP1 |
Gene Name | LAP1 |
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 | MKLLSVLALSATATSVLGASIPVDARAEKFLIELAPGETRWVTEEEKWELKRKGQDFFDITDEEVGFTAAVAQPAIAYPTSIRHANAVNAMIATLSKENMQRDLTKLSSFQTAYYKVDFGKQSATWLQEQVQAAINTAGANRYGAKVASFRHNFAQHSIIATIPGRSPEVVVVGAHQDSINQRSPMTGRAPGADDNGSGSVTILEALRGVLRDQTILQGKAANTIEFHWYAGEEAGLLGSQAIFANYKQTGKKVKGMLNQDMTGYIKGMVDKGLKVSFGIITDNVNANLTKFVRMVITKYCSIPTIDTRCGYACSDHASANRNGYPSAMVAESPIDLLDPHLHTDSDNISYLDFDHMIEHAKLIVGFVTELAK |
Enzyme Length | 373 |
Uniprot Accession Number | Q5QHG5 |
Absorption | |
Active Site | |
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 which contributes to pathogenicity. {ECO:0000250, 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 | Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (6); Signal peptide (1) |
Keywords | Aminopeptidase;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Secreted;Signal;Virulence;Zinc |
Interact With | |
Induction | INDUCTION: Expression is strongly increased during growth on protein-rich medium. Expressed at even higher levels when keratin is present 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..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 40,635 |
Kinetics | |
Metal Binding | METAL 176; /note=Zinc 1; /evidence=ECO:0000250; METAL 195; /note=Zinc 1; /evidence=ECO:0000250; METAL 195; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 234; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 261; /note=Zinc 1; /evidence=ECO:0000250; METAL 343; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |