| IED ID | IndEnz0002000477 |
| Enzyme Type ID | protease000477 |
| Protein Name |
Penicillopepsin-1 EC 3.4.23.20 Aspartic protease Peptidase A |
| Gene Name | |
| Organism | Penicillium janthinellum (Penicillium vitale) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium janthinellum (Penicillium vitale) |
| Enzyme Sequence | AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQQSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQAVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQPLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTAGSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCSTNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGDIFLKSQYVVFDSDGPQLGFAPQA |
| Enzyme Length | 323 |
| Uniprot Accession Number | P00798 |
| Absorption | |
| Active Site | ACT_SITE 33; /evidence="ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000269|PubMed:5475460"; ACT_SITE 213; /evidence="ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000269|PubMed:5475460" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.; EC=3.4.23.20; Evidence={ECO:0000269|PubMed:4946839}; |
| DNA Binding | |
| EC Number | 3.4.23.20 |
| Enzyme Function | FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'. {ECO:0000269|PubMed:4946839}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (27); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Helix (11); Sequence conflict (2); Turn (2) |
| Keywords | 3D-structure;Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01972}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (14) |
| Cross Reference PDB | 1APT; 1APU; 1APV; 1APW; 1BXO; 1BXQ; 1PPK; 1PPL; 1PPM; 2WEA; 2WEB; 2WEC; 2WED; 3APP; |
| Mapped Pubmed ID | 1567842; 1606144; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,461 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.20; |