Detail Information for IndEnz0002015954
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