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Gene Review

PHYH  -  phytanoyl-CoA 2-hydroxylase

Homo sapiens

Synonyms: LN1, LNAP1, PAHX, PHYH1, PhyH, ...
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Disease relevance of PHYH


High impact information on PHYH


Chemical compound and disease context of PHYH


Biological context of PHYH

  • Linkage analysis of a few patients diagnosed with RD, but without mutations in PHYH, suggested a second locus on chromosome 6q22-24 [8].
  • To enable mutation analysis of RD at the genome level, we have elucidated the genomic organization of the PHYH gene [11].
  • The A2 domain (337-740 amino acids) of factor VIII (FVIII-A2) was used as a bait and phytanoyl-CoA alpha-hydroxylase (PAHX) was identified as a binding protein of FVIII-A2 [12].
  • The middle portion (amino acids 83-264) of PAHX was used as a bait and a mouse brain cDNA library was searched [13].
  • Six mutations, including a large in-frame deletion and five missense mutations, were expressed in the yeast Saccharomyces cerevisiae to study their effect on PhyH activity [11].

Anatomical context of PHYH

  • In seven cases (4 NS, 2 LP, 1 LD) the monomorphic growths possessed a B-cell phenotype (LCA, L26, and LN1 positive; Leu-M1 and UCHL1 negative) [14].
  • The panel included four reagents recognizing probable T-cell and B-cell restricted leukocyte common moieties (UCHL1, MT1, MB1, 4KB5), three antibodies to B-cell-related antigens (KiB3, MB2, LN1), and one to a macrophage-related antigen (Mac411) [15].
  • Anti-alpha 6 antibodies inhibited adhesion to the LN-1/E8 fragment, but not to whole laminin or heat-denatured Laminin-1, indicating that chondrocytes utilize at least two beta 1-integrins for laminin adhesion, one of which is alpha 6 beta 1 recognizing the LN-1/E8 fragment [16].
  • Several polyclonal antibodies raised against laminin-1 or the LN-1/E8 fragment revealed a strong pericellular reaction in sections of human fetal epiphyseal cartilage and adult articular cartilage [16].
  • Binding of BSp73AS-1B1 to LN5 and, less markedly, LN1 induced spreading, lamellipodia formation and migration [17].

Associations of PHYH with chemical compounds


Other interactions of PHYH


Analytical, diagnostic and therapeutic context of PHYH

  • Northern and Western blot analyses demonstrated a unique pattern of developmental PAHX-AP #1 expression which was targeted to the adult brain, but ubiquitous expressions of PAHX were observed in all examined tissues [13].
  • We have identified a novel protein (PAHX-AP #1) associated with phytanoyl-CoA alpha-hydroxylase (PAHX), a Refsum disease gene product, using the yeast-based two-hybrid assay [13].
  • Subcellular localization studies using equilibrium density centrifugation showed that PhyH is indeed a peroxisomal protein in rat [21].
  • We have purified PhyH from rat liver to apparent homogeneity as judged by SDS-PAGE [21].
  • The monoclonal antibodies LN1, LN2, and L26 have been recently developed to recognize B-cell-specific antigens that survive routine tissue processing and paraffin embedding [5].


  1. Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7). Jansen, G.A., Waterham, H.R., Wanders, R.J. Hum. Mutat. (2004) [Pubmed]
  2. Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. Chambraud, B., Radanyi, C., Camonis, J.H., Rajkowski, K., Schumacher, M., Baulieu, E.E. Proc. Natl. Acad. Sci. U.S.A. (1999) [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. Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Fujinaga, K., Irwin, D., Huang, Y., Taube, R., Kurosu, T., Peterlin, B.M. Mol. Cell. Biol. (2004) [Pubmed]
  5. Monoclonal antibodies marking B-cell non-Hodgkin's lymphoma in paraffin-embedded tissue. Linder, J., Ye, Y., Armitage, J.O., Weisenburger, D.D. Mod. Pathol. (1988) [Pubmed]
  6. Identification of PAHX, a Refsum disease gene. Mihalik, S.J., Morrell, J.C., Kim, D., Sacksteder, K.A., Watkins, P.A., Gould, S.J. Nat. Genet. (1997) [Pubmed]
  7. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Jansen, G.A., Ofman, R., Ferdinandusse, S., Ijlst, L., Muijsers, A.O., Skjeldal, O.H., Stokke, O., Jakobs, C., Besley, G.T., Wraith, J.E., Wanders, R.J. Nat. Genet. (1997) [Pubmed]
  8. Identification of PEX7 as the second gene involved in Refsum disease. van den Brink, D.M., Brites, P., Haasjes, J., Wierzbicki, A.S., Mitchell, J., Lambert-Hamill, M., de Belleroche, J., Jansen, G.A., Waterham, H.R., Wanders, R.J. Am. J. Hum. Genet. (2003) [Pubmed]
  9. Comparing myotoxic effects of squalene synthase inhibitor, T-91485, and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors in human myocytes. Nishimoto, T., Tozawa, R., Amano, Y., Wada, T., Imura, Y., Sugiyama, Y. Biochem. Pharmacol. (2003) [Pubmed]
  10. Phytanic acid oxidase deficiency in childhood. Wise, G.A., Duffy, B.J., Mitchell, J.D., Pollard, A.C., Poulos, A., Pollard, J. Clinical and experimental neurology. (1985) [Pubmed]
  11. 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]
  12. Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII. Chen, C., Wang, Q., Fang, X., Xu, Q., Chi, C., Gu, J. J. Biol. Chem. (2001) [Pubmed]
  13. Identification of a brain specific protein that associates with a refsum disease gene product, phytanoyl-CoA alpha-hydroxylase. Lee, Z.H., Kim, H., Ahn, K.Y., Seo, K.H., Kim, J.K., Bae, C.S., Kim, K.K. Brain Res. Mol. Brain Res. (2000) [Pubmed]
  14. Monomorphic lymphomas arising in patients with Hodgkin's disease. Correlation of morphologic, immunophenotypic, and molecular genetic findings in 12 cases. Casey, T.T., Cousar, J.B., Mangum, M., Williams, M.E., Lee, J.T., Greer, J.P., Collins, R.D. Am. J. Pathol. (1990) [Pubmed]
  15. Detailed phenotypic analysis of B-cell lymphoma using a panel of antibodies reactive in routinely fixed wax-embedded tissue. Norton, A.J., Isaacson, P.G. Am. J. Pathol. (1987) [Pubmed]
  16. Identification and immunolocalization of laminin in cartilage. Dürr, J., Lammi, P., Goodman, S.L., Aigner, T., von der Mark, K. Exp. Cell Res. (1996) [Pubmed]
  17. Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin-3 and supports cell migration. Paret, C., Bourouba, M., Beer, A., Miyazaki, K., Schnölzer, M., Fiedler, S., Zöller, M. Int. J. Cancer (2005) [Pubmed]
  18. Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease. McDonough, M.A., Kavanagh, K.L., Butler, D., Searls, T., Oppermann, U., Schofield, C.J. J. Biol. Chem. (2005) [Pubmed]
  19. 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]
  20. Cerebro-hepato-renal (Zellweger) syndrome, adrenoleukodystrophy, and Refsum's disease: plasma changes and skin fibroblast phytanic acid oxidase. Poulos, A., Sharp, P., Fellenberg, A.J., Danks, D.M. Hum. Genet. (1985) [Pubmed]
  21. 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]
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