Pheophorbide a oxygenase (EC 1.14.15.17, pheide a monooxygenase, pheide a oxygenase, PAO) is an enzyme with systematic name pheophorbide-a,NADPH:oxygen oxidoreductase (biladiene-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
| Pheophorbide a oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.15.17 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Pheophorbide a + NADPH + H+ + O2 red chlorophyll catabolite + NADP+
Pheophorbide a oxygenase participates in chlorophyll degradation. Loss-of-function mutations in the gene can lead to a stay-green phenotype in plants.[7]
References
edit- ^ Hörtensteiner S, Wüthrich KL, Matile P, Ongania KH, Kräutler B (June 1998). "The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase". The Journal of Biological Chemistry. 273 (25): 15335–9. doi:10.1074/jbc.273.25.15335. PMID 9624113.
- ^ Pruzinská A, Tanner G, Anders I, Roca M, Hörtensteiner S (December 2003). "Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene". Proceedings of the National Academy of Sciences of the United States of America. 100 (25): 15259–64. doi:10.1073/pnas.2036571100. PMC 299977. PMID 14657372.
- ^ Chung DW, Pruzinská A, Hörtensteiner S, Ort DR (September 2006). "The role of pheophorbide a oxygenase expression and activity in the canola green seed problem". Plant Physiology. 142 (1): 88–97. doi:10.1104/pp.106.084483. PMC 1557622. PMID 16844830.
- ^ Rodoni S, Muhlecker W, Anderl M, Krautler B, Moser D, Thomas H, Matile P, Hortensteiner S (October 1997). "Chlorophyll Breakdown in Senescent Chloroplasts (Cleavage of Pheophorbide a in Two Enzymic Steps)". Plant Physiology. 115 (2): 669–676. doi:10.1104/pp.115.2.669. PMC 158527. PMID 12223835.
- ^ Hörtensteiner S (2006). "Chlorophyll degradation during senescence". Annual Review of Plant Biology. 57: 55–77. doi:10.1146/annurev.arplant.57.032905.105212. PMID 16669755.
- ^ Pruzinská A, Anders I, Aubry S, Schenk N, Tapernoux-Lüthi E, Müller T, Kräutler B, Hörtensteiner S (January 2007). "In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown". The Plant Cell. 19 (1): 369–87. doi:10.1105/tpc.106.044404. PMC 1820978. PMID 17237353.
- ^ Bachmann, Andre; Fernandez-Lopez, Jose; Ginsburg, Samuel; Thomas, Howard; Bouwcamp, John C; Solomos, Theophanes; Matile, Phillipe (1994). "Stay-green genotypes of Phaseolus vulgaris L.: chloroplast proteins and chlorophyll catabolites during foliar senescence". New Phytologist. 126 (4): 593–600. doi:10.1111/j.1469-8137.1994.tb02953.x.
External links
edit- Pheophorbide+a+oxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
