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; |