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Chemical Compound Review

porphobilinogen     3-[5-(aminomethyl)-4- (carboxymethyl)-1H...

Synonyms: SureCN188532, AG-J-05118, CHEBI:17381, P1134_SIGMA, HMDB00245, ...
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Disease relevance of porphobilinogen


High impact information on porphobilinogen


Chemical compound and disease context of porphobilinogen


Biological context of porphobilinogen


Anatomical context of porphobilinogen

  • Uroporphyrinogen I (URO) synthase [porphobilinogen ammonia-lyase (polymerizing), EC] activity increased when cultures of normal human bone marrow cells were incubated with erythropoietin [21].
  • Rabbit reticulocyte ALA-D is about as active in converting delta-aminolevulinic acid to porphobilinogen and as Zn2+-dependent as ALA-D purified from other sources [22].
  • ALA dehydratase activity, but not PBG deaminase activity or haem content, was markedly decreased in lymphocyte preparations from both patients with homozygous enzyme deficiency, and moderately decreased in subjects heterozygous for enzyme deficiency [23].
  • Diagnostic laboratory tests include quantitation of delta ALA, porphobilinogen, and porphyrins in blood, urine, and feces and analysis of activities of enzymes of the heme-forming system [24].
  • Ontogeny of 5-aminolevulinic dehydratase and porphobilinogen deaminase activities in the yolk sac membrane and liver of chick embryos [25].

Associations of porphobilinogen with other chemical compounds


Gene context of porphobilinogen


Analytical, diagnostic and therapeutic context of porphobilinogen


  1. Acute intermittent porphyria: characterization of a novel mutation in the structural gene for porphobilinogen deaminase. Demonstration of noncatalytic enzyme intermediates stabilized by bound substrate. Desnick, R.J., Ostasiewicz, L.T., Tishler, P.A., Mustajoki, P. J. Clin. Invest. (1985) [Pubmed]
  2. Acute intermittent porphyria: clinical and selected research aspects. Tschudy, D.P., Valsamis, M., Magnussen, C.R. Ann. Intern. Med. (1975) [Pubmed]
  3. Tissue-specific splicing mutation in acute intermittent porphyria. Grandchamp, B., Picat, C., Mignotte, V., Wilson, J.H., Te Velde, K., Sandkuyl, L., Roméo, P.H., Goossens, M., Nordmann, Y. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  4. Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria. Puy, H., Deybach, J.C., Lamoril, J., Robreau, A.M., Da Silva, V., Gouya, L., Grandchamp, B., Nordmann, Y. Am. J. Hum. Genet. (1997) [Pubmed]
  5. Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. Petrovich, R.M., Litwin, S., Jaffe, E.K. J. Biol. Chem. (1996) [Pubmed]
  6. Allosteric inhibition of human lymphoblast and purified porphobilinogen deaminase by protoporphyrinogen and coproporphyrinogen. A possible mechanism for the acute attack of variegate porphyria. Meissner, P., Adams, P., Kirsch, R. J. Clin. Invest. (1993) [Pubmed]
  7. Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria. Delfau, M.H., Picat, C., de Rooij, F.W., Hamer, K., Bogard, M., Wilson, J.H., Deybach, J.C., Nordmann, Y., Grandchamp, B. J. Clin. Invest. (1990) [Pubmed]
  8. Tin protoporphyrin prolongs the biochemical remission produced by heme arginate in acute hepatic porphyria. Dover, S.B., Moore, M.R., Fitzsimmons, E.J., Graham, A., McColl, K.E. Gastroenterology (1993) [Pubmed]
  9. X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase. Erskine, P.T., Senior, N., Awan, S., Lambert, R., Lewis, G., Tickle, I.J., Sarwar, M., Spencer, P., Thomas, P., Warren, M.J., Shoolingin-Jordan, P.M., Wood, S.P., Cooper, J.B. Nat. Struct. Biol. (1997) [Pubmed]
  10. Expression and subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in light-grown Euglena gracilis and three nonchlorophyllous cell lines. Shashidhara, L.S., Smith, A.G. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  11. Normal erythrocyte uroporphyrinogen I synthase in a kindred with acute intermittent porphyria. Mustajoki, P. Ann. Intern. Med. (1981) [Pubmed]
  12. Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. Thomas, S.D., Jordan, P.M. Nucleic Acids Res. (1986) [Pubmed]
  13. Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism. Frère, F., Schubert, W.D., Stauffer, F., Frankenberg, N., Neier, R., Jahn, D., Heinz, D.W. J. Mol. Biol. (2002) [Pubmed]
  14. Acute intermittent porphyria, seizures, and antiepileptic drugs: a report on a 3-year-old Nigerian boy. Sykes, R.M. Seizure : the journal of the British Epilepsy Association. (2001) [Pubmed]
  15. Failure of delta-aminolaevulinic acid and porphobilinogen to alter renal salt and water excretion in the dog. Unikowsky, B., Levy, M. Can. J. Physiol. Pharmacol. (1983) [Pubmed]
  16. DNA polymorphism of human porphobilinogen deaminase gene in acute intermittent porphyria. Llewellyn, D.H., Elder, G.H., Kalsheker, N.A., Marsh, O.W., Harrison, P.R., Grandchamp, B., Picat, C., Nordmann, Y., Romeo, P.H., Goossens, M. Lancet (1987) [Pubmed]
  17. Structure and expression of the Chlorobium vibrioforme hemB gene and characterization of its encoded enzyme, porphobilinogen synthase. Rhie, G., Avissar, Y.J., Beale, S.I. J. Biol. Chem. (1996) [Pubmed]
  18. Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors. Frère, F., Nentwich, M., Gacond, S., Heinz, D.W., Neier, R., Frankenberg-Dinkel, N. Biochemistry (2006) [Pubmed]
  19. Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions. Kervinen, J., Dunbrack, R.L., Litwin, S., Martins, J., Scarrow, R.C., Volin, M., Yeung, A.T., Yoon, E., Jaffe, E.K. Biochemistry (2000) [Pubmed]
  20. Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics. Williams, D.C., Morgan, G.S., McDonald, E., Battersby, A.R. Biochem. J. (1981) [Pubmed]
  21. Uroporphyrinogen I synthase induction in normal human bone marrow cultures: an early and quantitative response of erythroid differentiation. Sassa, S., Urabe, A. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  22. Purification of a 38-kDa protein from rabbit reticulocyte lysate which promotes protein renaturation by heat shock protein 70 and its identification as delta-aminolevulinic acid dehydratase and as a putative DnaJ protein. Gross, M., Hessefort, S., Olin, A. J. Biol. Chem. (1999) [Pubmed]
  23. Hereditary hepatic porphyria due to homozygous delta-aminolevulinic acid dehydratase deficiency: studies in lymphocytes and erythrocytes. Sassa, S., Fujita, H., Doss, M., Hassoun, A., Verstraeten, L., Mercelis, R., Kappas, A. Eur. J. Clin. Invest. (1991) [Pubmed]
  24. The porphyrias [corrected]: characteristics and laboratory tests. Ellefson, R.D., Ford, R.E. Regulatory toxicology and pharmacology : RTP. (1996) [Pubmed]
  25. Ontogeny of 5-aminolevulinic dehydratase and porphobilinogen deaminase activities in the yolk sac membrane and liver of chick embryos. Pauza, N.L., Sopena de Kracoff, Y.E., Ferramola de Sancovich, A.M., Sancovich, H.A. Br. Poult. Sci. (2002) [Pubmed]
  26. X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution. Erskine, P.T., Norton, E., Cooper, J.B., Lambert, R., Coker, A., Lewis, G., Spencer, P., Sarwar, M., Wood, S.P., Warren, M.J., Shoolingin-Jordan, P.M. Biochemistry (1999) [Pubmed]
  27. Reconstitution of the holoenzyme form of Escherichia coli porphobilinogen deaminase from apoenzyme with porphobilinogen and preuroporphyrinogen: a study using circular dichroism spectroscopy. Awan, S.J., Siligardi, G., Shoolingin-Jordan, P.M., Warren, M.J. Biochemistry (1997) [Pubmed]
  28. A spot test for uroporphyrinogen I synthase, the enzyme that is deficient in intermittent acute porphyria. Schumaker, H.M., Tishler, P.V., Knighton, D.J. Clin. Chem. (1976) [Pubmed]
  29. Familial porphyria cutanea tarda: the pattern of porphyrins formed from porphobilinogen by hemolysates. Alleman, M.A., Wilson, J.H., van den Berg, J.W., Edixhoven-Bosdijk, A., van Gastel-Quist, L.M. Clin. Chem. (1982) [Pubmed]
  30. Cloning and characterization of the hemA region of the Bacillus subtilis chromosome. Petricek, M., Rutberg, L., Schröder, I., Hederstedt, L. J. Bacteriol. (1990) [Pubmed]
  31. Structure and regulation of yeast HEM3, the gene for porphobilinogen deaminase. Keng, T., Richard, C., Larocque, R. Mol. Gen. Genet. (1992) [Pubmed]
  32. A role for HEM2 in cadmium tolerance. Hunter, T.C., Mehra, R.K. J. Inorg. Biochem. (1998) [Pubmed]
  33. Erythropoietin controls heme metabolic enzymes in normal human bone marrow culture. Abraham, N.G., Nelson, J.C., Ahmed, T., Konwalinka, G., Levere, R.D. Exp. Hematol. (1989) [Pubmed]
  34. Metal-induced alterations of delta-aminolevulinic acid dehydratase. Bernard, A., Lauwerys, R. Ann. N. Y. Acad. Sci. (1987) [Pubmed]
  35. Rare structural variants of human and murine uroporphyrinogen I synthase. Meisler, M.H., Carter, M.L. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  36. PK 11195 aggravates 3,5-diethoxycarbonyl-1,4-dihydrocollidine-induced hepatic porphyria in rats. Fonia, O., Weizman, R., Coleman, R., Kaganovskaya, E., Gavish, M. Hepatology (1996) [Pubmed]
  37. Dissection of the early steps in the porphobilinogen synthase catalyzed reaction. Requirements for Schiff's base formation. Jaffe, E.K., Hanes, D. J. Biol. Chem. (1986) [Pubmed]
  38. Determination of 5-aminolaevulinic acid dehydratase activity in erythrocytes and porphobilinogen in urine by micellar electrokinetic capillary chromatography. Luo, J.L., Deka, J., Lim, C.K. Journal of chromatography. A. (1996) [Pubmed]
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