Human phytanoyl-CoA hydroxylase: Resolution of the gene structure and the molecular basis of Refsum's disease

Human Molecular Genetics

Volumn 9, Issue 8, 2000, Pages 1195-1200

  Jansen, Gerbert A ^a   Hogenhout, Eveline M ^b   Ferdinandusse, Sacha ^b   Waterham, Hans R ^a   Ofman, Rob ^b   Jakobs, Cornelis ^c   Skjeldal, Ola H ^d   Wanders, Ronald J A ^a,b  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b Lab for Genetic Metabolic Diseases   (Netherlands)

^c VU UNIVERSITY MEDICAL CENTER   (Netherlands)

^d OSLO UNIVERSITY HOSPITAL   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

OXYGENASE; PHYTANIC ACID; PHYTANOYL COA HYDROXYLASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DRUG DEGRADATION; DRUG OXIDATION; ENZYME ACTIVITY; ENZYME DEFICIENCY; EXON; GENE DELETION; GENE FREQUENCY; GENE INSERTION; GENE STRUCTURE; HUMAN; HUMAN CELL; INTRON; MISSENSE MUTATION; MOLECULAR GENETICS; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN EXPRESSION; REFSUM DISEASE;

SACCHAROMYCES CEREVISIAE;

EID: 0034193437     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/9.8.1195     Document Type: Article

References (22)

1. Steinberg, D. (1995) In Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle, D. (eds), The Metabolic and Molecular Bases of Inherited Disease. McGraw-Hill, New York, NY, Vol. II, pp. 2351-2369.
2. Wanders, R.J.A. and Tager, J.M. (1998) Lipid metabolism in peroxisomes in relation to human disease. Mol. Aspects Med., 19, 71-154.
3. Verhoeven, N.M., Wanders, R.J.A., Poll-The, B.T., Saudubray, J.M. and Jakobs, C. (1998) The metabolism of phytanic acid and pristanic acid in man: a review. J. Inherit. Metab. Dis., 21, 697-728.
4. Watkins, P.A., Howard, A.E. and Mihalik, S.J. (1994) Phytanic acid must be activated to phytanoyl-CoA prior to its α-oxidation in rat liver peroxisomes. Biochim. Biophys. Acta, 1214, 288-294.
5. Mihalik, S.J., Rainville, A.M. and Watkins, P.A. (1995) Phytanic acid α-oxidation in rat liver peroxisomes. Production of α-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem., 232, 545-551.
6. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Moser, H.W., Jakobs, C., Denis, S. and Wanders, R.J.A. (1996) Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes, and deficient in Zellweger syndrome: direct, unequivocal evidence for the new, revised pathway of phytanic acid α-oxidation in humans. Biochem. Biophys Res. Commun., 229, 205-210.
7. Verhoeven, N.M., Schor, D.S.M., ten Brink, H.J., Wanders, R.J.A. and Jakobs, C. (1997) Resolution of the phytanic acid α-oxidation pathway - identification of pristanal as product of the decarboxylation of 2-hydroxyphytanoyl-CoA. Biochem. Biophys Res. Commun., 237, 33-36.
8. Croes, K., Van Veldhoven, P.P., Mannaerts, G.P. and Casteels, M. (1997) Production of formyl-CoA during peroxisomal α-oxidation of 3-methyl-branched fatty acids. FEBS Lett., 407, 197-200.
9. Croes, K., Casteels, M., Asselberghs, S., Herdewijn, P., Mannaerts, G.P. and Van Veldhoven, P.P. (1997) Formation of a 2-methyl-branched fatty aldehyde during peroxisomal α-oxidation. FEBS Lett., 412, 643-645.
10. Jansen, G.A., Verhoeven, N.M., Denis, S., Romeyn, G.J., Jakobs, C., ten Brink, H.J. and Wanders, R.J.A. (1999) Phytanic acid α-oxidation: identification of 2-hydroxyphytanoyl-CoA lyase in rat liver and its localisation in peroxisomes. Biochim. Biophys. Acta, 1440, 176-182.
11. Foulon, V., Antonenkov, V.D., Croes, K., Waelkens, E., Mannaerts, G.P., Van Veldhoven, P.P. and Casteels, M. (1999) Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during α-oxidation of 3-methyl-branched fatty acids. Proc. Natl Acad. Sci. USA, 96, 10039-10044.
12. Verhoeven, N.M., Wanders, R.J.A., Schor, D.S.M., Jansen, G.A. and Jakobs, C. (1997) Phytanic acid α-oxidation: decarboxylation of 2-hydroxyphytanoyl-CoA to pristanic acid in human liver. J. Lipid Res., 38, 2062-2070.
13. Jansen, G.A., Wanders, R.J.A., Watkins, P.A. and Mihalik, S.J. (1997) Phytanoyl-Coenzyme A hydroxylase deficiency: the enzyme defect in Refsum's disease. N. Engl. J. Med., 337, 133-134.
14. Jansen, G.A., Ofman, R., Ferdinandusse, S., Ijlst, L., Muijsers, A.O., Skjeldal, O.H., Stokke, O., Jakobs, C., Besley, G.T.N., Wraith, J.E. and Wanders, R.J.A. (1997) Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nature Genet., 17, 190-193.
15. Mihalik, S.J., Morrell, J.C., Kim, D., Sacksteder, K.A., Watkins, P.A. and Gould, S.J. (1997) Identification of PAHX, a Refsum disease gene. Nature Genet., 17, 185-189.
16. Jansen, G.A., Ferdinandusse, S., Skjeldal, O.H., Stokke, O., De Groot, C.J., Jakobs, C. and Wanders, R.J.A. (1998) Molecular basis of Refsum disease: identification of new mutations in the phytanoyl-CoA hydroxylase cDNA. J. Inherit. Metab. Dis., 21, 288-291.
17. Chahal, A., Khan, M., Pai, S.G., Barbosa, E. and Singh, I. (1998) Restoration of phytanic acid oxidation in Refsum disease fibroblasts from patients with mutations in the phytanoyl-CoA hydroxylase gene. FEBS Lett., 429, 119-122.
18. Seeburg, P.H., Colby, W.W., Capon, D.J., Goeddel, D.V. and Levinson, A.D. (1984) Biological properties of human c-Ha-ras1 genes mutated at codon 12. Nature, 312, 71-75.
19. Skjeldal, O.H., Stokke, O., Refsum, S., Norseth, J. and Petit, H. (1987) Clinical and biochemical heterogeneity in conditions with phytanic acid accumulation. J. Neurol. Sci., 77, 87-96.
20. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Jakobs, C., Moser, H.W. and Wanders, R.J.A. (1998) Characterization of phytanoyl-coenzyme A hydroxylase in human liver and activity measurements in patients with peroxisomal disorders. Clin. Chim. Acta, 271, 203-211.
21. Elgersma, Y., Van Den Berg, M., Tabak, H.F. and Distel, B. (1993) An efficient positive selection procedure for the isolation of peroxisomal import and peroxisome assembly mutants of Saccharomyces cerevisiae. Genetics, 135, 731-740.
22. Jones, E.W. (1977) Proteinase mutants of Saccharomyces cerevisiae. Genetics, 85, 23-33.