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Phytanoyl-CoA 2-hydroxylase

LN1, PAHX, phytanoyl-CoA hydroxylase, phytanic acid oxidase, PHYH
This gene is a member of the PhyH family and encodes a peroxisomal protein that is involved in the alpha-oxidation of 3-methyl branched fatty acids. Specifically, this protein converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. Mutations in this gene have been associated with Refsum disease (RD) and deficient protein activity has been associated with Zellweger syndrome and rhizomelic chondrodysplasia punctata. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, PGP 9.5, CAN, MT1
Papers using LN1 antibodies
Direct in vivo VH to JH rearrangement violating the 12/23 rule
Rajewsky Klaus et al., In The Journal of Experimental Medicine, 1993
... Genomic DNA was prepared from LN1 ES cells (6) using the Genomic DNA Kit according to the manufacturer's instructions (QIAGEN).
Papers on LN1
Physiological and pathological left ventricular hypertrophy of comparable degree is associated with characteristic differences of in vivo hemodynamics.
Radovits et al., Heidelberg, Germany. In Am J Physiol Heart Circ Physiol, Jan 2016
We aimed at investigating and comparing hemodynamic alterations in well established rat models of physiological (PhyH) and pathological hypertrophy (PaH) by using LV pressure-volume (P-V) analysis.
A derivatization approach using pyrylium salts for the sensitive and simple determination of sulfide in spring water by high performance liquid chromatography.
Zakrzewski et al., Łódź, Poland. In J Chromatogr A, Sep 2015
A high-performance liquid chromatography method based on pre-column derivatization with the pyrylium salts (4-[p-(N,N-dimethylamino)phenyl]-2,6-diphenylpyrylium perchlorate (LN1) and 2,4,6-triphenylpyrylium tetrafluoroborate (L1)) has been developed for the determination of sulfide.
Integrin α6β1 Expressed in ESCs Instructs the Differentiation to Endothelial Cells.
Malik et al., Chicago, United States. In Stem Cells, Jun 2015
Here, we investigated the inductive role of binding of integrin α6β1 expressed in mouse (m)ESCs to laminin-1 (LN1) in mediating the differentiation of ESCs to endothelial cells (ECs).
Adjuvant chemotherapy may improve survival of patients with luminal A breast cancer and positive lymph nodes.
Fan et al., Beijing, China. In Genet Mol Res, 2014
In the LN0 and LN1 subgroups, there was a trend towards an increased risk of death in patients receiving chemotherapy.
Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galβ1-3/4GlcNAc.
Lin et al., Taipei, Taiwan. In Plos One, 2014
Galectins represent β-galactoside-binding proteins and are known to bind Galβ1-3/4GlcNAc disaccharides (abbreviated as LN1 and LN2, respectively).
Cerebellar transcriptional alterations with Purkinje cell dysfunction and loss in mice lacking PGC-1α.
Cowell et al., Birmingham, United States. In Front Cell Neurosci, 2013
We found significant reductions in transcripts with synaptic (complexin1, Cplx1; Pacsin2), structural (neurofilament heavy chain, Nefh), and metabolic (isocitrate dehydrogenase 3a, Idh3a; neutral cholesterol ester hydrolase 1, Nceh1; pyruvate dehydrogenase alpha 1, Pdha1; phytanoyl-CoA hydroxylase, Phyh; ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1, Uqcrfs1) functions.
Peroxisomal disorders.
Wanders et al., Paris, France. In Handb Clin Neurol, 2012
The single peroxisomal enzyme deficiency group comprises seven different disorders, of which D-bifunctional protein and phytanoyl-CoA hydroxylase (adult Refsum disease) deficiencies are the most frequent.
Non-manifesting Refsum heterozygotes carrying the c.135-2A>G PAHX gene transition.
Voigtländer et al., Vienna, Austria. In Neurol Sci, 2008
In the absence of elevated phytanic acid concentrations, clinical neurologic abnormalities in heterozygous relatives of Refsum patients are not attributable to heterozygosity for PAHX mutations.
Structural and mechanistic studies on the peroxisomal oxygenase phytanoyl-CoA 2-hydroxylase (PhyH).
McDonough et al., Oxford, United Kingdom. In Biochem Soc Trans, 2007
PhyH (phytanoyl-CoA 2-hydroxylase, also known as PAHX), an Fe(II) and 2OG (2-oxoglutarate) oxygenase, catalyses hydroxylation of phytanoyl-CoA.
Refsum Disease
Leroy et al., Seattle, United States. In Unknown Journal, 2006
Confirmation of the diagnosis requires either (1) molecular genetic testing to identify biallelic pathogenic variants in either PHYH (encoding phytanoyl-CoA hydroxylase), which accounts for more than 90% of Refsum disease, or PEX7 (encoding the PTS2 receptor), which accounts for less than 10% of Refsum disease; or (2) enzyme analysis to identify deficiency of either phytanoyl-CoA hydroxylase enzyme activity or the peroxisome-targeting signal type 2 receptor.
Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.
Schofield et al., Oxford, United Kingdom. In J Biol Chem, 2006
manner in which phytanoyl-CoA 2-hydroxylase (PAHX) binds to iron(II) and 2-oxoglutarate at its active site distinguishes it from that of the other human 2-oxoglutarate (2OG)-dependent oxygenase
Prognostic value of extracapsular tumor spread for locoregional control in premenopausal patients with node-positive breast cancer treated with classical cyclophosphamide, methotrexate, and fluorouracil: long-term observations from International Breast Cancer Study Group Trial VI.
International Breast Cancer Study Group et al., Switzerland. In J Clin Oncol, 2005
PURPOSE: We sought to determine retrospectively whether extracapsular spread (ECS) might identify a subgroup that could benefit from radiotherapy after mastectomy, especially patients with 1 to 3 positive lymph nodes (LN1-3+).
Studies on the specificity of unprocessed and mature forms of phytanoyl-CoA 2-hydroxylase and mutation of the iron binding ligands.
Schofield et al., Oxford, United Kingdom. In J Lipid Res, 2005
demonstrate that both unprocessed and processed forms are able to hydroxylate a range of CoA derivatives; site-directed mutagenesis was used to support proposals for the identity of the iron binding istes of PAHX
Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7).
Wanders et al., Amsterdam, Netherlands. In Hum Mutat, 2004
Ten novel PHYH mutations found in Refsum disease patients.
Further studies on the substrate spectrum of phytanoyl-CoA hydroxylase: implications for Refsum disease?
Van Veldhoven et al., Leuven, Belgium. In J Lipid Res, 2003
substrate specificity of PAHX is broader than expected, so Refsum disease might be characterized by an accumulation of not only phytanic acid but also other 3-alkyl-branched fatty acids
Alpha-oxidation of 3-methyl-substituted fatty acids and its thiamine dependence.
Van Veldhoven et al., Leuven, Belgium. In Eur J Biochem, 2003
Human pathology due to a deficient alpha-oxidation is mostly linked to mutations in the gene coding for the second enzyme of the sequence, phytanoyl-CoA hydroxylase.
Identification of PAHX, a Refsum disease gene.
Gould et al., Baltimore, United States. In Nat Genet, 1997
Human PAHX is targetted to peroxisomes, requires the PTS2 receptor for peroxisomal localization, interacts with the PTS2 receptor in the yeast two-hybrid assay and has intrinsic phytanoyl-CoA alpha-hydroxylase activity that requires the dioxygenase cofactor iron and cosubstrate 2-oxoglutarate.
Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene.
Wanders et al., Amsterdam, Netherlands. In Nat Genet, 1997
Biochemically, the disease is caused by the deficiency of phytanoyl-CoA hydroxylase (PhyH), a peroxisomal protein catalyzing the first step in the alpha-oxidation of phytanic acid.
Further evidence that "malignant angioendotheliomatosis" is an angiotropic large-cell lymphoma.
Rappaport et al., In N Engl J Med, 1986
A detailed antigenic phenotyping of neoplastic lymphoid cells showed that one patient had the immunophenotype T11+, Leu-1+, Leu-3+, Leu-2+, B1-, B2-, SIg-, LN1-, LN2-, the predominant phenotype for peripheral T-cell lymphoma; the others had T11-, Leu-1-, Leu-3-, Leu-2-, B1+, B2+, SIg+, LN1+, LN2+, consistent with a B-cell-derived lymphoma.
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