| IED ID | IndEnz0002015425 |
| Enzyme Type ID | protease015425 |
| Protein Name |
probable leucine aminopeptidase 2 EC 3.4.11.- Aminopeptidase II Leucyl aminopeptidase 2 LAP2 |
| Gene Name | lap2 AO090003000354 |
| 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 | MRSLLWASLLSGVLAGRALVSPDEFPEDIQLEDLLEGSQQLEDFAYAYPERNRVFGGKAHDDTVNYLYEELKKTGYYDVYKQPQVHLWSNADQTLKVGDEEIEAKTMTYSPSVEVTADVAVVKNLGCSEADYPSDVEGKVALIKRGECPFGDKSVLAAKAKAAASIVYNNVAGSMAGTLGAAQSDKGPYSAIVGISLEDGQKLIKLAEAGSVSVDLWVDSKQENRTTYNVVAQTKGGDPNNVVALGGHTDSVEAGPGINDDGSGIISNLVIAKALTQYSVKNAVRFLFWTAEEFGLLGSNYYVSHLNATELNKIRLYLNFDMIASPNYALMIYDGDGSAFNQSGPAGSAQIEKLFEDYYDSIDLPHIPTQFDGRSDYEAFILNGIPSGGLFTGAEGIMSEENASRWGGQAGVAYDANYHAAGDNMTNLNHEAFLINSKATAFAVATYANDLSSIPKRNTTSSLHRRARTMRPFGKRAPKTHAHVSGSGCWHSQVEA |
| Enzyme Length | 496 |
| Uniprot Accession Number | Q2ULM2 |
| Absorption | |
| Active Site | ACT_SITE 292; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | |
| 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. {ECO:0000269|PubMed:10899618}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Retains 65 and 46 percent residual activity after a 20 min incubation at 70 and 75 degrees Celsius, respectively. {ECO:0000269|PubMed:10899618}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:10899618}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (6); Metal binding (6); Region (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10899618}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000269|PubMed:10899618 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,557 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 mM for Leu-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=9 mM for Lys-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=3.5 mM for Ala-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=1.5 mM for Glu-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=13 mM for Val-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=15 mM for Pro-paranitroanilide {ECO:0000269|PubMed:10899618}; KM=51 mM for Ile-paranitroanilide {ECO:0000269|PubMed:10899618}; |
| Metal Binding | METAL 248; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 260; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 260; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 293; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 321; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 419; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda |