IED ID | IndEnz0002000367 |
Enzyme Type ID | protease000367 |
Protein Name |
Philibertain g 1 EC 3.4.22.- Philibertain g I Fragment |
Gene Name | |
Organism | Philibertia gilliesii (Milkweed) (Sarcostemma gilliesii) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Gentianales Apocynaceae Asclepiadoideae Asclepiadeae MOOG clade Oxypetalinae Philibertia Philibertia gilliesii (Milkweed) (Sarcostemma gilliesii) |
Enzyme Sequence | LPASVDWRKEGAVLPIRHQGQCG |
Enzyme Length | 23 |
Uniprot Accession Number | P84789 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the cysteine protease inhibitor E-64. Not inhibited by the serine protease inhibitor PMSF, the aspartic protease inhibitor pepstatin A, or by the metal ion chelator 1,10-phenanthroline. {ECO:0000269|PubMed:16328737}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Thiol protease. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for casein is 7.6 and philibertain g 1 retains more than 80% of maximum activity between pH 6.7 and pH 8.7, and 50% of maximum activity between pH 6.1 and pH 9.8. Optimum pH for PFLNA is 6.2-7.2 and philibertain g I retains more than 80% of maximum activity between pH 5.8 and pH 7.8, and 50% of maximum activity between pH 5.2 and pH 8.6. {ECO:0000269|PubMed:16328737}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Non-terminal residue (1) |
Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 2,518 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for PFLNA {ECO:0000269|PubMed:16328737}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |