| IED ID | IndEnz0002000915 |
| Enzyme Type ID | protease000915 |
| Protein Name |
Physarolisin EC 3.4.21.103 Physaropepsin Cleaved into: Physarolisin heavy chain; Physarolisin light chain |
| Gene Name | |
| Organism | Physarum polycephalum (Slime mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Myxogastria (plasmodial slime molds) Myxogastromycetidae Physariida Physaraceae Physarum Physarum polycephalum (Slime mold) |
| Enzyme Sequence | MRLLSLLFLLGLATLSFAVRSQWAQQGRATHEALITIRFALTQQNLDVLERTLLDISDTTSKNYGKWKTAEEVTELVAPAREISERVASFLERQGATKVENFRDMVKVTAPVSWIEETLHTNLFFFQHKTRTSKVIIRADGGYKIPAEIAEHVDFVAGLFEFPSIKNARTQVGAGVDGYIVPYVIFDLYGIPTTFPVHPNSSICLVEFQDDQSYNKDDLKKFAKENEITETVVSHTVGPYSGSSADTESTLDVQYGGAIALNTTVWFWTVEDWMYDFATDFLNTKNPPLVVSMSWGWPEPEQCQVGNCTGDETSLEYVVRTNVEFQKIGAIGTTLLAASGDQGAPGDSDPECNSKKKPLSSIFPGASPWVLSVGATMLSNMTTEDADPSAEPPICKSWTCSTSTTELVCTIPQALITTGGGFSDYSLQPSYQNAAVAAYFKSGVPLPPQTDFNASNRGFPDVSALGHNYLIALSGDFEQVDGTSASTPVFAAIIAHLNSYRLNNGKPPLAFAVPLIYQAFASDPTIFNDITTGDNKCTEDCCSKFGYEATKGWDPVTGVGTPVFSKLLAFVQTLP |
| Enzyme Length | 575 |
| Uniprot Accession Number | Q8MZS4 |
| Absorption | |
| Active Site | ACT_SITE 248; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 252; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 484; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and diazoacetyl-D,L-norleucine methyl ester (DAN). {ECO:0000269|PubMed:12589815, ECO:0000269|PubMed:2246266}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)(2).; EC=3.4.21.103; Evidence={ECO:0000269|PubMed:2246266}; |
| DNA Binding | |
| EC Number | 3.4.21.103 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 1.7 with hemoglogin as substrate. {ECO:0000269|PubMed:12589815}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Domain (1); Glycosylation (5); Metal binding (4); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Protease;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autocatalytically processed.; PTM: N-glycosylated. {ECO:0000269|PubMed:2246266}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 62,709 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.3 uM for Lys-Pro-Ile-Glu-Phe+Phe(NO(2))-Arg-Leu {ECO:0000269|PubMed:2246266}; |
| Metal Binding | METAL 529; /note=Calcium; /evidence=ECO:0000250; METAL 530; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 552; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 554; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.103; |