| IED ID | IndEnz0002014133 |
| Enzyme Type ID | protease014133 |
| Protein Name |
Aorsin EC 3.4.21.- |
| Gene Name | aorO AO090026000083 |
| 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 | MRPLSHLSFFNGLLLGLSALSAATSVVHERREATSSNWVKRARVNPSDKHVVRIGLTQSSLEEAHDLLMDVSNPSSPNYARFYSADEVAAKFAPSTETVNEVQNWLTEKGINASRVAQTQNHGWLVFHATSKEIENLFDTTYYEYHNRKTGKKAIACEQYHVPASVQKHIDYVHPGVNLNPSSGKPSSIRRRAAASKKTKLPARGPRPIQQHDVKGLNVTNCDQLITPECIRALYKIPSARAAPHPNNSLGIFEEGDYYAQEDLDLFFKTFAKDIPQGTHPIPAFIDGAEAPVPVTKAGGESDLDFELAYPIVHPQSITLYQTDDANWASNTTGFLNTFLDALDGSYCTYCAYGECGNDPSLDPVYPDDAGYDGQLMCGVFKPTNVISVSYGEQENDLPANYQQRQCMEFLKLGLQGVSVLFASGDNGVAGPPGDGNSVNGCLNNGTVFSPAFPNSCPYITNVGATKVYPGYTVSQPESAVYDPDGLYSYASGGGFSNIYPIPDYQAEAVATYFKDHNPPYPYYEGAENLGKNGGLYNRLGRGYPDVAANGDNIAVFNGGEFGSSGGTSASTPIFASIINRIIDERLAVGKGPVGFINPVLYKNPSVLNDITNGTNPGCGTDGFSTAPGWDPATGLGTPNYPKMLKLWLDLP |
| Enzyme Length | 652 |
| Uniprot Accession Number | Q8NK92 |
| Absorption | |
| Active Site | ACT_SITE 301; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P42790; ACT_SITE 305; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P42790; ACT_SITE 569; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P42790 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by antipain and leupeptin. {ECO:0000269|PubMed:12519073}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine endopeptidase which hydrolyzes a range of fluorogenic peptide substrates containing the basic residues arginine or lysine at the P1 position and prefers paired basic resides. Also hydrolyzes clupeine and salmine, activates plasminogen and converts trypsinogen to trypsin. {ECO:0000269|PubMed:12519073}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Remains fully active after heating at 50 degrees Celsius and pH 4.0 for 10 min. Retains 65% of its activity after heating at 55 degrees Celsius for 10 min. The half-life value for loss of activity at 60 degrees Celsius and pH 4.0 is 3.5 min. {ECO:0000269|PubMed:12519073}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. Inactive below pH 3.0 and above pH 6.5. The half-life (t1/2) values for activity loss at 30 degrees Celsius are 150 min at pH 6.6, 5.5 min at pH 6.8 and 14 min at pH 2.4. {ECO:0000269|PubMed:12519073}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (6); Metal binding (4); Mutagenesis (8); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:12519073}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:12519073}.; PTM: O-glycosylated. {ECO:0000303|PubMed:12519073, ECO:0000305}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,501 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 uM for Boc-Gln-Arg-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=3.9 uM for Boc-Leu-Arg-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=2.8 uM for Boc-Gly-Arg-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=10.0 uM for Boc-Leu-Lys-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=26.8 uM for Boc-Gly-Lys-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=58.0 uM for Boc-Leu-Thr-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=84.5 uM for Boc-Leu-Gly-Arg-MCA {ECO:0000269|PubMed:12519073}; KM=88.3 uM for Boc-Gln-Gly-Arg-MCA {ECO:0000269|PubMed:12519073}; Vmax=12.8 nmol/sec/mg enzyme with Z-Arg-Arg-MCA as substrate {ECO:0000269|PubMed:12519073}; Note=The highest catalytic efficiency is observed for Boc-Leu-Lys-Arg-MCA. {ECO:0000269|PubMed:12519073}; |
| Metal Binding | METAL 610; /note=Calcium; /evidence=ECO:0000269|PubMed:12519073; METAL 611; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 629; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 631; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |