| IED ID | IndEnz0002000634 |
| Enzyme Type ID | protease000634 |
| Protein Name |
Pepsin A EC 3.4.23.1 |
| Gene Name | PGA |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA |
| Enzyme Length | 385 |
| Uniprot Accession Number | P00791 |
| Absorption | |
| Active Site | ACT_SITE 91; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:1097438, ECO:0000269|PubMed:4897201"; ACT_SITE 274; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:1097438, ECO:0000269|PubMed:4897201" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10094}; |
| DNA Binding | |
| EC Number | 3.4.23.1 |
| Enzyme Function | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (28); Chain (1); Disulfide bond (3); Domain (1); Helix (16); Modified residue (1); Mutagenesis (1); Propeptide (1); Sequence conflict (8); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Aspartyl protease;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Phosphoprotein;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 127; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03954 |
| Post Translational Modification | PTM: Minor amounts of the active enzyme occur with 'Ala-58' at the amino end. |
| Signal Peptide | SIGNAL 1..15; /evidence="ECO:0000269|PubMed:2494172, ECO:0000269|PubMed:3044927, ECO:0000269|PubMed:4584879, ECO:0000269|PubMed:4881358" |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 1F34; 1PSA; 1YX9; 2PSG; 3PEP; 3PSG; 4PEP; 5PEP; 6XCT; 6XCY; 6XCZ; 6XD2; |
| Mapped Pubmed ID | 10932249; 1418819; 15883044; 19367902; 19481105; 19715777; 2115087; 32001282; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,262 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.1; |