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Chemical Compound Review

AGN-PC-00IWML     [5-(6-aminopurin-9-yl)-4- hydroxy-2...

Synonyms: AC1L194G, Phytanoyl-CoA (triethylammonium salt)
 
 
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Disease relevance of CPD-206

 

High impact information on CPD-206

  • These results corresponded to high-affinity binding of phytanoyl-CoA to the recombinant rat SCP2 protein, as well as high 3-ketopristanoyl-CoA thiolase activity of the recombinant rat SCPx protein [2].
  • Further characterization supported that the gene disruption led to inefficient import of phytanoyl-CoA into peroxisomes and to defective thiolytic cleavage of 3-ketopristanoyl-CoA [2].
  • The H175A and D177A mutants did not catalyse hydroxylation of phytanoyl-CoA, consistent with their assigned role as iron(II) binding ligands [3].
  • Although pristanic and phytanic acids were rapidly converted to pristanoyl-CoA and phytanoyl-CoA, respectively, they were not converted to carnitine esters by mitochondrial outer membranes [4].
  • Phytanoyl-CoA is efficiently 2-hydroxylated by PAHX in vitro in the presence of mature SCP-2 [5].
 

Chemical compound and disease context of CPD-206

 

Biological context of CPD-206

 

Anatomical context of CPD-206

 

Associations of CPD-206 with other chemical compounds

 

Gene context of CPD-206

 

Analytical, diagnostic and therapeutic context of CPD-206

References

  1. Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease. Jansen, G.A., Hogenhout, E.M., Ferdinandusse, S., Waterham, H.R., Ofman, R., Jakobs, C., Skjeldal, O.H., Wanders, R.J. Hum. Mol. Genet. (2000) [Pubmed]
  2. Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice lacking the sterol carrier protein-2/sterol carrier protein-x gene function. Seedorf, U., Raabe, M., Ellinghaus, P., Kannenberg, F., Fobker, M., Engel, T., Denis, S., Wouters, F., Wirtz, K.W., Wanders, R.J., Maeda, N., Assmann, G. Genes Dev. (1998) [Pubmed]
  3. Structure-function analysis of phytanoyl-CoA 2-hydroxylase mutations causing Refsum's disease. Mukherji, M., Chien, W., Kershaw, N.J., Clifton, I.J., Schofield, C.J., Wierzbicki, A.S., Lloyd, M.D. Hum. Mol. Genet. (2001) [Pubmed]
  4. Peroxisomal beta-oxidation of branched chain fatty acids in rat liver. Evidence that carnitine palmitoyltransferase I prevents transport of branched chain fatty acids into mitochondria. Singh, H., Beckman, K., Poulos, A. J. Biol. Chem. (1994) [Pubmed]
  5. Utilization of sterol carrier protein-2 by phytanoyl-CoA 2-hydroxylase in the peroxisomal alpha oxidation of phytanic acid. Mukherji, M., Kershaw, N.J., Schofield, C.J., Wierzbicki, A.S., Lloyd, M.D. Chem. Biol. (2002) [Pubmed]
  6. Restoration of phytanic acid oxidation in Refsum disease fibroblasts from patients with mutations in the phytanoyl-CoA hydroxylase gene. Chahal, A., Khan, M., Pai, S.G., Barbosa, E., Singh, I. FEBS Lett. (1998) [Pubmed]
  7. Phytanoyl-CoA ligase activity in rat liver. Muralidharan, F.N., Muralidharan, V.B. Biochem. Int. (1986) [Pubmed]
  8. Refsum disease: a defect in the alpha-oxidation of phytanic acid in peroxisomes. Singh, I., Pahan, K., Singh, A.K., Barbosa, E. J. Lipid Res. (1993) [Pubmed]
  9. Phytanoyl-CoA hydroxylase activity is induced by phytanic acid. Zomer, A.W., Jansen, G.A., Van Der Burg, B., Verhoeven, N.M., Jakobs, C., Van Der Saag, P.T., Wanders, R.J., Poll-The, B.T. Eur. J. Biochem. (2000) [Pubmed]
  10. Phytanic acid alpha-oxidation in rat liver mitochondria. Pahan, K., Gulati, S., Singh, I. Biochim. Biophys. Acta (1994) [Pubmed]
  11. Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. Pahan, K., Singh, I. J. Lipid Res. (1995) [Pubmed]
  12. Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-coAs and requirement for GTP or ATP and Mg(2+) in addition to its known hydroxylation cofactors. Croes, K., Foulon, V., Casteels, M., Van Veldhoven, P.P., Mannaerts, G.P. J. Lipid Res. (2000) [Pubmed]
  13. Phytanic acid must be activated to phytanoyl-CoA prior to its alpha-oxidation in rat liver peroxisomes. Watkins, P.A., Howard, A.E., Mihalik, S.J. Biochim. Biophys. Acta (1994) [Pubmed]
  14. Phytanoyl-CoA hydroxylase from rat liver. Protein purification and cDNA cloning with implications for the subcellular localization of phytanic acid alpha-oxidation. Jansen, G.A., Ofman, R., Denis, S., Ferdinandusse, S., Hogenhout, E.M., Jakobs, C., Wanders, R.J. J. Lipid Res. (1999) [Pubmed]
  15. Studies on phytanoyl-CoA 2-hydroxylase and synthesis of phytanoyl-coenzyme A. Kershaw, N.J., Mukherji, M., MacKinnon, C.H., Claridge, T.D., Odell, B., Wierzbicki, A.S., Lloyd, M.D., Schofield, C.J. Bioorg. Med. Chem. Lett. (2001) [Pubmed]
  16. Phytanic acid activation in rat liver peroxisomes is catalyzed by long-chain acyl-CoA synthetase. Watkins, P.A., Howard, A.E., Gould, S.J., Avigan, J., Mihalik, S.J. J. Lipid Res. (1996) [Pubmed]
  17. Peroxisomal trans-2-enoyl-CoA reductase is involved in phytol degradation. Gloerich, J., Ruiter, J.P., van den Brink, D.M., Ofman, R., Ferdinandusse, S., Wanders, R.J. FEBS Lett. (2006) [Pubmed]
 
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