Pheophorbide a oxygenase

Pheophorbide A oxygenase (EC 1.14.12.20, 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 + NADPH + H⁺ + O₂

\rightleftharpoons

red chlorophyll catabolite + NADP⁺

Pheophorbide A oxygenase participates in chlorophyll degradation.

References

↑ Hörtensteiner, S., Wüthrich, K.L., Matile, P., Ongania, K.H. and Kräutler, B. (1998). "The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase". J. Biol. Chem. 273 (25): 15335–15339. doi:10.1074/jbc.273.25.15335. PMID 9624113.
↑ Pružinská, A., Tanner, G., Anders, I., Roca, M. and Hörtensteiner, S. (2003). "Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene". Proc. Natl. Acad. Sci. USA 100 (25): 15259–15264. doi:10.1073/pnas.2036571100. PMC 299977. PMID 14657372.
↑ Chung, D.W., Pružinská, A., Hörtensteiner, S. and Ort, D.R. (2006). "The role of pheophorbide a oxygenase expression and activity in the canola green seed problem". Plant Physiol. 142 (1): 88–97. doi:10.1104/pp.106.084483. PMC 1557622. PMID 16844830.
↑ Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. (1997). "Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps". Plant Physiol. 115 (2): 669–676. doi:10.1104/pp.115.2.669. PMC 158527. PMID 12223835.
↑ Hörtensteiner, S. (2006). "Chlorophyll degradation during senescence". Annu. Rev. Plant Biol. 57: 55–77. doi:10.1146/annurev.arplant.57.032905.105212. PMID 16669755.
↑ Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. (2007). "In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown". Plant Cell 19 (1): 369–387. doi:10.1105/tpc.106.044404. PMC 1820978. PMID 17237353.

External links

Pheophorbide a oxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase

1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase

1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1

1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1

1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase

1.14.17: reduced ascorbate	Dopamine beta-hydroxylase

1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1

1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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