| IED ID | IndEnz0018001354 |
| Enzyme Type ID | peroxidase001354 |
| Protein Name |
Peroxygenase 1 AsPXG1 EC 1.11.2.3 |
| Gene Name | |
| Organism | Avena sativa (Oat) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Poodae Poeae Aveninae Avena Avena sativa (Oat) |
| Enzyme Sequence | MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH |
| Enzyme Length | 249 |
| Uniprot Accession Number | G1JSL4 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by beta-mercaptoethanol and organophosphorothioates such as parathion or terbufos. {ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:21784965}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3; Evidence={ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885, ECO:0000269|PubMed:21784965}; |
| DNA Binding | |
| EC Number | 1.11.2.3 |
| Enzyme Function | FUNCTION: Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors. {ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885, ECO:0000269|PubMed:21784965}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:21784965}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21784965}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (5); Motif (1) |
| Keywords | Calcium;Direct protein sequencing;Endoplasmic reticulum;Heme;Iron;Lipid droplet;Membrane;Metal-binding;Microsome;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 124..133; /note=Proline-knot |
| Gene Encoded By | |
| Mass | 28,107 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.07 uM for 9-HPOD {ECO:0000269|PubMed:21784965}; KM=10.42 uM for 9-HPOT {ECO:0000269|PubMed:21784965}; KM=25.18 uM for 13-HPOD {ECO:0000269|PubMed:21784965}; KM=7.25 uM for 13-HPOT {ECO:0000269|PubMed:21784965}; KM=215.76 uM for cumene hydroperoxide {ECO:0000269|PubMed:21784965}; Vmax=214.04 pmol/sec/mg enzyme toward 9-HPOD {ECO:0000269|PubMed:21784965}; Vmax=188.69 pmol/sec/mg enzyme toward 9-HPOT {ECO:0000269|PubMed:21784965}; Vmax=306.57 pmol/sec/mg enzyme toward 13-HPOD {ECO:0000269|PubMed:21784965}; Vmax=173.49 pmol/sec/mg enzyme toward 13-HPOT {ECO:0000269|PubMed:21784965}; Vmax=883.34 pmol/sec/mg enzyme toward cumene hydroperoxide {ECO:0000269|PubMed:21784965}; |
| Metal Binding | METAL 76; /note=Iron (heme axial ligand); /evidence=ECO:0000250; METAL 81; /note=Calcium; /evidence=ECO:0000255; METAL 83; /note=Calcium; /evidence=ECO:0000255; METAL 85; /note=Calcium; /evidence=ECO:0000255; METAL 92; /note=Calcium; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda | 1.11.2.3; |