| IED ID | IndEnz0002013722 |
| Enzyme Type ID | protease013722 |
| Protein Name |
Leucine aminopeptidase A EC 3.4.11.- Leucyl aminopeptidase A LAPA |
| Gene Name | lapA AO090011000052 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MRFLPCIATLAATASALAIGDHVRSDDQYVLELAPGQTKVVTEAEKWALRAEGKRFFDITERASSLELASNKKQKLAVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAHQDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL |
| Enzyme Length | 377 |
| Uniprot Accession Number | Q2U1F3 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Calcium, magnesium and manganese cations reduce peptidase activity to 20.3-51.3 percent. The metal ion chelating reagent EDTA almost completely inhibits activity. The protease inhibitor bacitracin and the aminopeptidase B inhibitor bestatin, as well as DTT and beta-mercaptoethanol act also as lap A inhibitorsD. {ECO:0000269|PubMed:20803144}. |
| 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:20803144}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:20803144}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:20803144}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (6); Propeptide (1); Signal peptide (1) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expressed at higher level at alkaline conditions. May be under the control of pacC, the transcription factor that regulates pH-conditional gene expression. Expression is very low under normal condition, salt condition and heat-stress condition. {ECO:0000269|PubMed:20803144}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19129648, ECO:0000269|PubMed:20803144}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 6ZEP; 6ZEQ; 7OEZ; |
| Mapped Pubmed ID | 33989771; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,105 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.244 mM for Leu-p-nitroaniline {ECO:0000269|PubMed:20803144}; KM=0.782 mM for Phe-p-nitroaniline {ECO:0000269|PubMed:20803144}; |
| 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 |