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Gene Review

PPOX  -  protoporphyrinogen oxidase

Homo sapiens

Synonyms: PPO, Protoporphyrinogen oxidase, V290M, VP
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Disease relevance of PPOX


Psychiatry related information on PPOX

  • Following the optimization of the paste composition, PPO-based carbon paste biosensors were prepared and presented excellent analytical properties toward catechol detection with a sensitivity of 4.7 A M(-1) cm(-2) and a response time lower than 20 s [6].
  • The venturesome in both camps will be intrigued by General Telephone of California's comprehensive, managed mental health care program, combining the PPO concept with provider risk and strong case management, as described by the authors, Vice Presidents of Preferred Health Care, Ltd [7].
  • The case study presented here demonstrates the use of marketing principles which emphasize the importance of participation and communication in decision making with physicians in the formation of a PPO [8].

High impact information on PPOX


Chemical compound and disease context of PPOX


Biological context of PPOX


Anatomical context of PPOX


Associations of PPOX with chemical compounds

  • The NH2-terminal amino acid sequence of the deduced PPO contains a conserved amino acid sequence that forms the dinucleotide-binding site in many flavin-containing proteins [24].
  • This arginine residue is evolutionarily highly conserved in humans, mice, bacteria, yeast, and plants, indicating the importance of this residue in PPO [27].
  • Purified R59W lacks the FAD cofactor which may be explained by the fact that this mutation resides within the dinucleotide binding motif of PPO [28].
  • Protoporphyrinogen oxidase then converts the methylene-interrupted macrocycle of protoporphyrinogen IX into a conjugated system [29].
  • The data indicate that PPO and proteinase inhibitor genes are coactivated systemically by wounding via the octadecanoid signal transduction pathway and that systemin has a much broader role in signaling plant defensive genes than was previously known [30].

Other interactions of PPOX

  • Finally, we explored the functional consequences of polymorphisms on the abundance of wild-type RNA, and used relative allelic mRNA determinations to find out whether low-expressed HMBS, PPOX and the CPO alleles occur in the general population [21].
  • We constructed a structural model for the interaction between the amino-terminal end of PPOX and the putative mitochondrial receptor protein Tom20 [31].
  • Mapping of the 5' end PPOX mRNA by polymerase chain reaction indicated that there are the same transcripts in erythroid and nonerythroid cells [19].
  • Despite extensive mutation analysis, no other potential disease-causing genetic alterations could be detected in the PPOX gene or the uroporphyrinogen III synthase gene [32].
  • Furthermore, microsatellite markers flanking the PPOX and alpha-1 antitrypsin (PI) gene, on chromosomes 1 and 14, respectively, were used to assess the probability of involvement of these loci in disease presentation [33].

Analytical, diagnostic and therapeutic context of PPOX

  • Mutations in the PPOX gene were identified by a combination of screening (denaturing gradient gel electrophoresis, heteroduplex analysis, or denaturing high-performance liquid chromatography) and direct automated sequencing of amplified genomic DNA [1].
  • Sequence analysis revealed that the cDNA for Arabidopsis PPOX encodes a protein of 537 amino acids (aa) with a calculated molecular mass of 57.7 kDa [5].
  • Slight overrepresentation of the mutant PPOX allele was however, observed repeatedly in DNA of the proband compared to other R59W heterozygotes, including his mother who also tested positive for mutation R59W using restriction enzyme analysis and direct DNA sequencing [32].
  • Northern blot analysis revealed the synthesis of a 1.8-kilobase pair mRNA for PPO [24].
  • Protoporphyrinogen oxidase in cultures of Epstein-Barr virus transformed lymphoblasts from twenty-seven patients showed a mean maximal velocity (Vmax) of 0.39 +/- 0.08+ nmol of protoporphyrin mg protein-1 h-1, a 52% reduction (P less than 0.001) from a non-porphyric control group (0.82 +/- 0.10) [34].


  1. Variegate porphyria in Western Europe: identification of PPOX gene mutations in 104 families, extent of allelic heterogeneity, and absence of correlation between phenotype and type of mutation. Whatley, S.D., Puy, H., Morgan, R.R., Robreau, A.M., Roberts, A.G., Nordmann, Y., Elder, G.H., Deybach, J.C. Am. J. Hum. Genet. (1999) [Pubmed]
  2. Evidence for involvement of a second genetic locus on chromosome 11q in porphyrin metabolism. Norton, B., Lanyon, W.G., Moore, M.R., Porteous, M., Youngs, G.R., Connor, J.M. Hum. Genet. (1993) [Pubmed]
  3. Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase. Dailey, T.A., Woodruff, J.H., Dailey, H.A. Biochem. J. (2005) [Pubmed]
  4. Molecular characterization of homozygous variegate porphyria. Roberts, A.G., Puy, H., Dailey, T.A., Morgan, R.R., Whatley, S.D., Dailey, H.A., Martasek, P., Nordmann, Y., Deybach, J.C., Elder, G.H. Hum. Mol. Genet. (1998) [Pubmed]
  5. Molecular cloning and characterization of a cDNA that encodes protoporphyrinogen oxidase of Arabidopsis thaliana. Narita, S., Tanaka, R., Ito, T., Okada, K., Taketani, S., Inokuchi, H. Gene (1996) [Pubmed]
  6. Composite carbon paste biosensor for phenolic derivatives based on in situ electrogenerated polypyrrole binder. Mailley, P., Cummings, E.A., Mailley, S.C., Eggins, B.R., McAdams, E., Cosnier, S. Anal. Chem. (2003) [Pubmed]
  7. The next generation of managed mental health care. Rodriguez, A., Lee, F.C. Health cost management. (1987) [Pubmed]
  8. Monopolies, Maricopa, and marketing: a case study. Perkins, J., Mercer, A., McClary, C. Hospital & health services administration. (1986) [Pubmed]
  9. A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Meissner, P.N., Dailey, T.A., Hift, R.J., Ziman, M., Corrigall, A.V., Roberts, A.G., Meissner, D.M., Kirsch, R.E., Dailey, H.A. Nat. Genet. (1996) [Pubmed]
  10. Chester porphyria: biochemical studies of a new form of acute porphyria. McColl, K.E., Thompson, G.G., Moore, M.R., Goldberg, A., Church, S.E., Qadiri, M.R., Youngs, G.R. Lancet (1985) [Pubmed]
  11. Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. Koch, M., Breithaupt, C., Kiefersauer, R., Freigang, J., Huber, R., Messerschmidt, A. EMBO J. (2004) [Pubmed]
  12. Neuron-specific expression and physiological regulation of bovine vasopressin transgenes in mice. Ang, H.L., Carter, D.A., Murphy, D. EMBO J. (1993) [Pubmed]
  13. Kinetic and physical characterisation of recombinant wild-type and mutant human protoporphyrinogen oxidases. Maneli, M.H., Corrigall, A.V., Klump, H.H., Davids, L.M., Kirsch, R.E., Meissner, P.N. Biochim. Biophys. Acta (2003) [Pubmed]
  14. Recurrent missense mutation in the protoporphyrinogen oxidase gene underlies variegate porphyria. Frank, J., Jugert, F.K., Breitkopf, C., Goerz, G., Merk, H.F., Christiano, A.M. Am. J. Med. Genet. (1998) [Pubmed]
  15. Platelet factor 4 mRNA expression in cells from a patient with megakaryoblastic crisis of chronic myelogenous leukemia. Ryo, R., Adachi, M., Sugano, W., Yasunaga, M., Yoshida, A., Jikai, J., Saigo, K., Yamaguchi, N., Akita, H., Yokoyama, M. Cancer (1991) [Pubmed]
  16. Protoporphyrin IX fluorescence kinetics in C6 glioblastoma cells after delta-aminolevulinic acid incubation: effect of a protoporphyrinogen oxidase inhibitor. Carre, J., Eleouet, S., Rousset, N., Vonarx, V., Heyman, D., Lajat, Y., Patrice, T. Cell. Mol. Biol. (Noisy-le-grand) (1999) [Pubmed]
  17. A simple fluorimetric assay for pyridoxamine phosphate oxidase in erythrocyte haemolysates: effects of riboflavin supplementation and of glucose 6-phosphate dehydrogenase deficiency. Bates, C.J., Powers, H.J. Human nutrition. Clinical nutrition. (1985) [Pubmed]
  18. Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. Deybach, J.C., Puy, H., Robréau, A.M., Lamoril, J., Da Silva, V., Grandchamp, B., Nordmann, Y. Hum. Mol. Genet. (1996) [Pubmed]
  19. The human protoporphyrinogen oxidase gene (PPOX): organization and location to chromosome 1. Taketani, S., Inazawa, J., Abe, T., Furukawa, T., Kohno, H., Tokunaga, R., Nishimura, K., Inokuchi, H. Genomics (1995) [Pubmed]
  20. Clinical and biochemical characteristics and genotype-phenotype correlation in Finnish variegate porphyria patients. von und zu Fraunberg, M., Timonen, K., Mustajoki, P., Kauppinen, R. Eur. J. Hum. Genet. (2002) [Pubmed]
  21. Modulation of penetrance by the wild-type allele in dominantly inherited erythropoietic protoporphyria and acute hepatic porphyrias. Gouya, L., Puy, H., Robreau, A.M., Lyoumi, S., Lamoril, J., Da Silva, V., Grandchamp, B., Deybach, J.C. Hum. Genet. (2004) [Pubmed]
  22. Protoporphyrinogen oxidase: complete genomic sequence and polymorphisms in the human gene. Puy, H., Robréau, A.M., Rosipal, R., Nordmann, Y., Deybach, J.C. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  23. Identification of sequences required for the import of human protoporphyrinogen oxidase to mitochondria. Morgan, R.R., Errington, R., Elder, G.H. Biochem. J. (2004) [Pubmed]
  24. Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli. Nishimura, K., Taketani, S., Inokuchi, H. J. Biol. Chem. (1995) [Pubmed]
  25. Variant acute intermittent porphyria in a child. Badcock, N.R., Zoanetti, G.D., O'Reilly, D.A., Robertson, E.F. Clin. Chem. (1990) [Pubmed]
  26. The enzymatic defect in variegate prophyria. Studies with human cultured skin fibroblasts. Brenner, D.A., Bloomer, J.R. N. Engl. J. Med. (1980) [Pubmed]
  27. The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. Frank, J., Poh-Fitzpatrick, M.B., King, L.E., Christiano, A.M. Arch. Dermatol. Res. (1998) [Pubmed]
  28. Characteristics of human protoporphyrinogen oxidase in controls and variegate porphyrias. Dailey, H.A., Dailey, T.A. Cell. Mol. Biol. (Noisy-le-grand) (1997) [Pubmed]
  29. The modification of acetate and propionate side chains during the biosynthesis of haem and chlorophylls: mechanistic and stereochemical studies. Akhtar, M. Ciba Found. Symp. (1994) [Pubmed]
  30. Systemin activates synthesis of wound-inducible tomato leaf polyphenol oxidase via the octadecanoid defense signaling pathway. Constabel, C.P., Bergey, D.R., Ryan, C.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  31. Mitochondrial targeting of normal and mutant protoporphyrinogen oxidase. von und zu Fraunberg, M., Nyröen, T., Kauppinen, R. J. Biol. Chem. (2003) [Pubmed]
  32. Overrepresentation of the founder PPOX gene mutation R59W in a South African patient with severe clinical manifestation of porphyria. de Villiers, J.N., Kotze, M.J., van Heerden, C.J., Sadie, A., Gardner, H.F., Liebenberg, J., van Zyl, R., du Plessis, L., Kimberg, M., Frank, J., Warnich, L. Exp. Dermatol. (2005) [Pubmed]
  33. Molecular analysis reveals a high mutation frequency in the first untranslated exon of the PPOX gene and largely excludes variegate porphyria in a subset of clinically affected Afrikaner families. Kotze, M.J., De Villiers, J.N., Groenewald, J.Z., Rooney, R.N., Loubser, O., Thiart, R., Oosthuizen, C.J., van Niekerk, M.M., Groenewald, I.M., Retief, A.E., Warnich, L. Mol. Cell. Probes (1998) [Pubmed]
  34. Protoporphyrinogen oxidase and porphobilinogen deaminase in variegate porphyria. Meissner, P.N., Day, R.S., Moore, M.R., Disler, P.B., Harley, E. Eur. J. Clin. Invest. (1986) [Pubmed]
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