IED ID | IndEnz0002004089 |
Enzyme Type ID | protease004089 |
Protein Name |
Leucine aminopeptidase 1 EC 3.4.11.- Leucyl aminopeptidase 1 LAP1 |
Gene Name | lap1 |
Organism | Aspergillus sojae |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus sojae |
Enzyme Sequence | MRFLPCIATLAATASALAIGDHIRSDDQYVLELGPGETKVVTEAEKWALRAEGKRFFDITGRTSSLELASNKKQKLAVTYPDSVQHNETVQNLINSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHFFPQSSLIAKIPGKSDKTIVLGAHQDSINLNSPSEGRAPSADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYLQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKIIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL |
Enzyme Length | 377 |
Uniprot Accession Number | Q8J2N2 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Activity is strongly inhibited by metalchelating agents, such as EDTA and dipicolinic acid. {ECO:0000269|PubMed:12031491}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.11.- |
Enzyme Function | FUNCTION: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates. {ECO:0000269|PubMed:12031491}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:12031491}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.1-10. {ECO:0000269|PubMed:12031491}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (6); Propeptide (1); Signal peptide (1) |
Keywords | Aminopeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 41,179 |
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 | 3.4.11.1;3.4.11.22; |