IED ID | IndEnz0002000484 |
Enzyme Type ID | protease000484 |
Protein Name |
Penicillopepsin-2 EC 3.4.23.20 Aspartic protease pepA Penicillopepsin-JT2 |
Gene Name | pepA |
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 | MVVFSKITVVLAGLATVASAVPTGTSRKSTFTVNQKARPVAQAKAINLPGMYASALSKYGAAVPASVKAAAESGTAVTTPEANDVEYLTPVNVGGTTLNLDFDTGSADLWVFSSELSSSESTGHSLYKPSSNATKLAGYSWSITYGDQSSASGDVYKDFVVVGGVKASPQAVEAASQISQQFVNDKNNDGLLGLAFSSINTVKPKSQTTFFDTVKGQLDSPLFAVTLKHNAPGTYDFGFVDKNKYTGSLTYAQVDSSQGFWSFTADGYKIGSKSGGSIQGIADTGTTLLLLPDNVVSDYYGQVSGAQQDSSAGGYTVPCSAQLPDFTVTIGSYNAVVPGSLINYAPLQSGSSTCFGGIQSNSGLGFSIFGDIFLKSQYVVFDANGPRLGFAPQA |
Enzyme Length | 394 |
Uniprot Accession Number | P78735 |
Absorption | |
Active Site | ACT_SITE 103; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 283; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
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:10850809}; |
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:10850809}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
Keywords | Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01972}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 40,840 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for Ac-Lys-p-nitrophenylalanyl-amide {ECO:0000269|PubMed:10850809}; KM=0.4 mM for Ac-Ala-Lys-p-nitrophenylalanyl-amide {ECO:0000269|PubMed:10850809}; KM=0.5 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-amide {ECO:0000269|PubMed:10850809}; KM=0.59 mM for Ac-Lys-p-nitrophenylalanyl-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.5 mM for Ac-Ala-Lys-p-nitrophenylalanyl-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.35 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.21 mM for Ac-Lys-p-nitrophenylalanyl-Ala-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.41 mM for Ac-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.32 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide {ECO:0000269|PubMed:10850809}; KM=0.46 mM for Ac-Ala-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide {ECO:0000269|PubMed:10850809}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.23.20; |