| IED ID | IndEnz0002000356 |
| Enzyme Type ID | protease000356 |
| Protein Name |
Subtilisin-like serine protease Pen c 1 EC 3.4.21.- Alkaline serine protease allergen Pen c 1 |
| Gene Name | |
| Organism | Penicillium citrinum |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium citrinum |
| Enzyme Sequence | MGFLKVLATSLATLAVVDAGTLLTASNTDAVIPSSYIVVMNDDVSTAEFNTHREWATNVHARLSRRKNGETGPGKHFEINGLKGYTASFDESTAKDIANDPAVKYIEPDMIVNATANVVQSNVPSWGLARISSKRTGTTSYTYDSTAGEGVVFYGVDTGIDISHSDFGGRAKWGTNVVDNDNTDGNGHGTHTASTAAGSKYGVAKKATLVAVKVLGADGSGTNSGVISGMDWAVKDAKSRGANGKYVMNMSLGGEFSKAVNDAAANVVKSGIFLSVAAGNEAENASNSSPASAAEVCTIAASTSTDGSASFTNFGSVVDLYAPGQSITAAYPGGGSKTLSGTSMAAPHVAGVAAYLMALEGVSAGNACARIVQLATSSISRAPSGTTSKLLYNGINV |
| Enzyme Length | 397 |
| Uniprot Accession Number | Q9Y749 |
| Absorption | |
| Active Site | ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 188; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 343; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 0.1 mM diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), chymostatin and elastatinal. Not inhibited by N-alpha-p-tosyl-L-lysine chloromethylketone (TLCK), N-tosyl-L-phenylalanyl chloromethyl ketone (TPCK) or N-carbobenzoxy-L-phenylalanine chloromethylketone (ZPCK). {ECO:0000269|PubMed:7763554}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease (PubMed:10103041, PubMed:7763554). Hydrolyzes azocasein (PubMed:10103041). Cleaves peptide bonds of the oxidized insulin B chain preferably at 15-Leu-|-Tyr-16, but also at 4-Gln-|-His-5 and 24-Phe-|-Phe-25, and to a lesser extent at 5-His-|-Leu-6 and 25-Phe-|-Tyr-26. Hydrolyzes amide bonds between amino acids and 7-amino-4-methylcoumarin (AMC) in vitro (PubMed:7763554). {ECO:0000269|PubMed:10103041, ECO:0000269|PubMed:7763554}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Protease activity is retained up to 40 degrees Celsius for 30 min, but completely inactivated at 50 degrees Celsius (at pH 7). Activity is retained up to 25 degrees Celsius, and completely inactivated at 40 degrees Celsius (at pH 11). {ECO:0000269|PubMed:7763554}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active at pH 7 (up to 40 degrees Celsius for 30 min) and at pH 11 (up to 25 degrees Celsius). {ECO:0000269|PubMed:7763554}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Propeptide (1); Sequence conflict (3); Signal peptide (1); Site (4) |
| Keywords | Allergen;Direct protein sequencing;Hydrolase;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255, ECO:0000269|PubMed:10103041}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,384 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mM for t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide (Boc-VLK-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554}; KM=0.11 mM for t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide ((Boc-LSTR-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554}; KM=0.13 mM for succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.63; |