| IED ID | IndEnz0005000511 |
| Enzyme Type ID | lipase000511 |
| Protein Name |
Pheophorbidase RsPPD EC 3.1.1.82 |
| Gene Name | PPD |
| Organism | Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Brassiceae Raphanus Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus) |
| Enzyme Sequence | MGGEGGADDSVVHFVFVHGASHGAWCWYKLTTLLVAAGFKATSVDLTGAGINLTDSNTVFDFDHYNRPLFSLLSDLPSHHKIVLVGHSIGGGSVTEALCKFTDKISMVVYLAADMVQPGSTSSTHDSIMTVGEEDIWEYIYGEGADKPPTGVLMKEEFRRHYYYSQSPLEDVSLASKLLRPAPVRALGGADKLSPNPEAEKVPRVYIKTAKDNLFDPLRQDRLVEKWPPSQLYILEESDHSAFFSVPTTLFAYLLRAVSFLQL |
| Enzyme Length | 263 |
| Uniprot Accession Number | Q2V0W1 |
| Absorption | |
| Active Site | ACT_SITE 88; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 212; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by methanol and phenylmethylsulfonicfluoride (PMSF). |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H(+) + H2O + pheophorbide a = CO2 + methanol + pyropheophorbide a; Xref=Rhea:RHEA:32483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17790, ChEBI:CHEBI:58687, ChEBI:CHEBI:58742; EC=3.1.1.82; Evidence={ECO:0000269|PubMed:16228561, ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; |
| DNA Binding | |
| EC Number | 3.1.1.82 |
| Enzyme Function | FUNCTION: Involved in chlorophyll degradation. Specific for the pheophorbides of the dihydroporphyrin and tetrahydroporphyrin types. Chlorophyllide a, pheophytin a and the nonfluorescent chlorophyll catabolite (NCC) are not used as substrates. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for the native enzyme and 7.0-7.5 for the PPD-GST recombinant enzyme. {ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Chlorophyll catabolism;Cytoplasm;Direct protein sequencing;Hydrolase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Up-regulated by senescence. {ECO:0000269|PubMed:16384908}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,974 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.1 uM for pheophorbide a (for the native enzyme) {ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; KM=95.5 uM for pheophorbide a (for the PPD-GST recombinant enzyme) {ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; KM=240 uM for pheophorbide b (for the native enzyme) {ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; KM=40 uM for bacterio-pheophorbide a (for the native enzyme) {ECO:0000269|PubMed:16384908, ECO:0000269|PubMed:18846292}; |
| Metal Binding | |
| Rhea ID | RHEA:32483 |
| Cross Reference Brenda |