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Gene Review

FAH  -  fumarylacetoacetate hydrolase...

Homo sapiens

Synonyms: Beta-diketonase, FAA, Fumarylacetoacetase, Fumarylacetoacetate hydrolase
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Disease relevance of FAH


Psychiatry related information on FAH

  • The present study assessed the relationship between anxiety, as measured by the State-Trait Personality Inventory (STPI), and success of post-strike air traffic control specialist (ATCS) trainees at the FAA Academy and during field training [6].

High impact information on FAH

  • A single mutation of the fumarylacetoacetate hydrolase gene in French Canadians with hereditary tyrosinemia type I [7].
  • In all four patients the immunonegative liver tissue contained the FAH mutations demonstrated in fibroblasts of the patients [8].
  • In four patients exhibiting mosaicism of FAH protein, analysis for the tyrosinemia-causing mutations was performed in immunonegative and immunopositive areas of liver tissue by restriction digestion analysis and direct DNA sequencing [8].
  • These various molecular phenotypes suggest that this disorder may be caused by a variety of FAH mutations [1].
  • BACKGROUND AND AIMS: Hereditary tyrosinemia type I (HTI) is a recessively inherited disease caused by a deficiency of fumarylacetoacetate hydrolase (FAH), the last enzyme of the tyrosine catabolic pathway [9].

Chemical compound and disease context of FAH


Biological context of FAH


Anatomical context of FAH

  • In an individual homozygous for pseudodeficiency of FAH and in three HT1 families also carrying the pseudodeficiency allele, western blotting of fibroblast extracts showed that the pseudodeficiency allele gave very little immunoreactive FAH protein, whereas northern analysis revealed a normal amount of FAH mRNA [16].
  • No immunoreactive FAH band was observed on immunoblots of liver, kidneys, and lymphocytes from patients presenting with the acute form of hereditary tyrosinemia [17].
  • By this immunoblot assay, FAH was detected in most human tissues, with maximal immunoreactivity in liver and kidneys and with only trace amounts in chorionic villi and cultured amniocytes [17].
  • Immunoblot analysis of aborted fetal tissues revealed normal FAH immunoreactivity in normal liver and kidneys [17].
  • Site-directed mutagenesis and expression in a rabbit reticulocyte lysate system demonstrated that the C1021-->T mutation gave reduced FAH activity and reduced amounts of the full-length protein [16].

Associations of FAH with chemical compounds

  • In this pilot project, FAH was measured first, and, if necessary, succinylacetone was determined as the complementary test [18].
  • Fumarylacetoacetate hydrolase (FAH) is the terminal enzyme in the catabolic pathway of tyrosine [19].
  • Direct sequencing of the 14 exons of the FAH gene showed a G to A transition, which predicts a change from tryptophan to a stop codon (TGG-->TGA) at position 262 (W262X) [20].
  • The three FA analogues [12-(9-anthroyloxy)stearic acid, 5-doxylstearic acid, and 1-pyrenenonanoic acid] moved across PC bilayers via the un-ionized form; except for the anthroyloxy FA (kappa FAH = 4.8 x 10(-3) s-1), the rates were too fast to measure (t 1/2 < 1 s) [21].
  • The related 2- furoylhydrazine ( FAH ) reacts at lower alkali concentrations, making this an attractive alternative carbohydrate reagent since it is (unlike PAHBAH ) freely water soluble [22].

Other interactions of FAH

  • This indicates that the single polypeptide chain encoded by the FAH gene contains all the genetic information required for functional activity, suggesting that the dimer found in vivo is a homodimer [15].
  • We used reverse transcription and the polymerase chain reaction to amplify the FAH cDNA of a 12-year-old American boy with chronic tyrosinemia type 1 [23].
  • Analysis of FAH expression in liver sections obtained after resection for hepatocellular carcinoma revealed a mosaic pattern of expression [24].
  • In tyrosinemia, these three hepatic enzyme activities were all decreased: TAT showed approximately 35%, p- HPPA oxidase 11%, and FAH 60% of the corresponding control values [25].
  • This study was aimed to evaluate the electromyographic behaviour of that musculature in patients while pronouncing the syllables PAH, BAH, MAH, SAH, FAH, VAH, MEE, and the word MISSISSIPPI [26].

Analytical, diagnostic and therapeutic context of FAH


  1. Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. Phaneuf, D., Lambert, M., Laframboise, R., Mitchell, G., Lettre, F., Tanguay, R.M. J. Clin. Invest. (1992) [Pubmed]
  2. Structural and functional analysis of missense mutations in fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia type 1. Bergeron, A., D'Astous, M., Timm, D.E., Tanguay, R.M. J. Biol. Chem. (2001) [Pubmed]
  3. Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase. Rootwelt, H., Chou, J., Gahl, W.A., Berger, R., Coşkun, T., Brodtkorb, E., Kvittingen, E.A. Hum. Genet. (1994) [Pubmed]
  4. Spectrum of mutations in the fumarylacetoacetate hydrolase gene of tyrosinemia type 1 patients in northwestern Europe and Mediterranean countries. Bergman, A.J., van den Berg, I.E., Brink, W., Poll-The, B.T., Ploos van Amstel, J.K., Berger, R. Hum. Mutat. (1998) [Pubmed]
  5. Urinary excretion of deuterated metabolites in patients with tyrosinemia type I after oral loading with deuterated L-tyrosine. Wadman, S.K., Duran, M., Ketting, D., Bruinvis, L., van Sprang, F.J., Berger, R., Smit, G.P., Steinmann, B., Leonard, J.V., Divry, P., Farriaux, J.P., Cartigny, B. Clin. Chim. Acta (1983) [Pubmed]
  6. Relationships of anxiety scores to screening and training status of air traffic controllers. Collins, W.E., Schroeder, D.J., Nye, L.G. Aviation, space, and environmental medicine. (1991) [Pubmed]
  7. A single mutation of the fumarylacetoacetate hydrolase gene in French Canadians with hereditary tyrosinemia type I. Grompe, M., St-Louis, M., Demers, S.I., al-Dhalimy, M., Leclerc, B., Tanguay, R.M. N. Engl. J. Med. (1994) [Pubmed]
  8. Self-induced correction of the genetic defect in tyrosinemia type I. Kvittingen, E.A., Rootwelt, H., Berger, R., Brandtzaeg, P. J. Clin. Invest. (1994) [Pubmed]
  9. No evidence of maternal cell colonization in reverted liver nodules of tyrosinemia type I patients. Bergeron, A., Lettre, F., Russo, P., Morissette, J., Tanguay, R.M. Gastroenterology (2004) [Pubmed]
  10. Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity. Labelle, Y., Phaneuf, D., Leclerc, B., Tanguay, R.M. Hum. Mol. Genet. (1993) [Pubmed]
  11. Crystal structure and mechanism of a carbon-carbon bond hydrolase. Timm, D.E., Mueller, H.A., Bhanumoorthy, P., Harp, J.M., Bunick, G.J. Structure (1999) [Pubmed]
  12. Hereditary tyrosinemia type I--an overview. Kvittingen, E.A. Scand. J. Clin. Lab. Invest. Suppl. (1986) [Pubmed]
  13. Biochemical studies on the enzymatic deficiencies in hereditary tyrosinemia. Berger, R., van Faassen, H., Smith, G.P. Clin. Chim. Acta (1983) [Pubmed]
  14. The amino acid factor in stone formers' and normal urines. Azoury, R., Garti, N., Sarig, S. Urol. Res. (1986) [Pubmed]
  15. Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15. Phaneuf, D., Labelle, Y., Bérubé, D., Arden, K., Cavenee, W., Gagné, R., Tanguay, R.M. Am. J. Hum. Genet. (1991) [Pubmed]
  16. Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I. Rootwelt, H., Brodtkorb, E., Kvittingen, E.A. Am. J. Hum. Genet. (1994) [Pubmed]
  17. Different molecular basis for fumarylacetoacetate hydrolase deficiency in the two clinical forms of hereditary tyrosinemia (type I). Tanguay, R.M., Valet, J.P., Lescault, A., Duband, J.L., Laberge, C., Lettre, F., Plante, M. Am. J. Hum. Genet. (1990) [Pubmed]
  18. Fumarylacetoacetase measurement as a mass-screening procedure for hereditary tyrosinemia type I. Laberge, C., Grenier, A., Valet, J.P., Morissette, J. Am. J. Hum. Genet. (1990) [Pubmed]
  19. Localization of cells in the rat brain expressing fumarylacetoacetate hydrolase, the deficient enzyme in hereditary tyrosinemia type 1. Labelle, Y., Puymirat, J., Tanguay, R.M. Biochim. Biophys. Acta (1993) [Pubmed]
  20. Identification of a stop mutation in five Finnish patients suffering from hereditary tyrosinemia type I. St-Louis, M., Leclerc, B., Laine, J., Salo, M.K., Holmberg, C., Tanguay, R.M. Hum. Mol. Genet. (1994) [Pubmed]
  21. Movement of fatty acids, fatty acid analogues, and bile acids across phospholipid bilayers. Kamp, F., Hamilton, J.A., Kamp, F., Westerhoff, H.V., Hamilton, J.A. Biochemistry (1993) [Pubmed]
  22. Optimal conditions for 4-hydroxybenzoyl- and 2-furoylhydrazine as reagents for the determination of carbohydrates, including ketosamines. Lever, M., Walmsley, T.A., Visser, R.S., Ryde, S.J. Anal. Biochem. (1984) [Pubmed]
  23. Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1. Hahn, S.H., Krasnewich, D., Brantly, M., Kvittingen, E.A., Gahl, W.A. Hum. Mutat. (1995) [Pubmed]
  24. A missense mutation (Q279R) in the fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosinemia, acts as a splicing mutation. Dreumont, N., Poudrier, J.A., Bergeron, A., Levy, H.L., Baklouti, F., Tanguay, R.M. BMC Genet. (2001) [Pubmed]
  25. Enzyme defect in a case of tyrosinemia type I, acute form. Furukawa, N., Kinugasa, A., Seo, T., Ishii, T., Ota, T., Machida, Y., Inoue, F., Imashuku, S., Kusunoki, T., Takamatsu, T. Pediatr. Res. (1984) [Pubmed]
  26. Electromyographic analysis of the upper and lower fascicles of the orbicular oris muscle, in edentulous patients, before and after complete denture implantation. Santos, C.M., Vitti, M., de Mattos, M.d.a. .G., Semprini, M., Paranhos, H.d.e. .F., Regalo, S.C. Electromyography and clinical neurophysiology. (2003) [Pubmed]
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