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Information on EC 1.14.11.18 - phytanoyl-CoA dioxygenase
for references in articles please use BRENDA:EC1.14.11.18
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
1.14.11.18 phytanoyl-CoA dioxygenase
IUBMB Comments
Part of the peroxisomal phytanic acid α-oxidation pathway. Requires Fe2+ and ascorbate.
The enzyme appears in viruses and cellular organisms
- 1.14.11.18
- peroxisomal
- refsum
-
alpha-oxidation
- zellweger
-
pigmentosa
-
beta-oxidation
-
3,7,11,15-tetramethylhexadecanoic
- punctata
-
pipecolic
-
rhizomelic
-
pristanic
- 2-hydroxyphytanoyl-coa
-
chondrodysplasia
-
2-hydroxylation
-
anosmia
-
3-methyl
- phytol
-
3-methyl-branched
-
cerebro-hepato-renal
-
2-oxoglutarate-dependent
- diagnostics
- medicine
Reaction Schemes
showSynonyms
phytanoyl-coa hydroxylase, phyhd1, phytanic acid oxidase, phytanoyl-coa 2-hydroxylase, phytanoyl-coa alpha-hydroxylase, phytanoyl-coa dioxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PAHX
PhyH
Phytanic acid oxidase
-
-
-
-
phytanoyl-CoA 2-hydroxylase
Phytanoyl-CoA alpha-hydroxylase
-
-
-
-
phytanoyl-CoA hydroxylase
-
-
-
-
PAHX
-
-
-
-
PhyH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Part of the peroxisomal phytanic acid alpha-oxidation pathway. Requires Fe2+ and ascorbate.
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CAS REGISTRY NUMBER
COMMENTARY
185402-46-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,7-dimethyloctan-6-enoyl-CoA + 2-oxoglutarate + O2
3,7-dimethyl-2-hydroxyocta-7-enoyl-CoA + succinate + CO2
-
Substrates: 75.2 of the activity with 3-methylhexadecanoyl-CoA
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3-ethylnonanoyl-CoA + 2-oxoglutarate + O2
3-ethoxy-2-hydroxyhexadecanoyl-CoA + succinate + CO2
-
Substrates: 64.7% of the activity with 3-methylhexadecanoyl-CoA
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3-methyl-5-phenyl-pentanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methyl-5-phenylpentanoyl-CoA + succinate + CO2
-
Substrates: 53% of the activity with 3-methylhexadecanoyl-CoA
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3-methyldodecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methyldodecanoyl-CoA + succinate + CO2
-
Substrates: 110% of the activity with 3-methylhexadecanoyl-CoA
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3-methylheptanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylheptanoyl-CoA + succinate + CO2
-
Substrates: 16.2% of the activity with 3-methylhexadecanoyl-CoA
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3-methylhexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylhexadecanoyl-CoA + succinate + CO2
3-methylnonanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylnonanoyl-CoA + succinate + CO2
-
Substrates: 111% of the activity with 3-methylhexadecanoyl-CoA
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3-methylundecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylundecanoyl-CoA + succinate + CO2
-
Substrates: 110% of the activity with 3-methylhexadecanoyl-CoA
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butanoyl-CoA + 2-oxoglutarate + O2
2-hydroxybutanoyl-CoA + succinate + CO2
-
Substrates: -
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?
decanoyl-CoA + 2-oxoglutarate + O2
2-hydroxydecanoyl-CoA + succinate + CO2
-
Substrates: -
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?
dodecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxydodecanoyl-CoA + succinate + CO2
-
Substrates: -
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?
hexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyhexadecanoyl-CoA + succinate + CO2
-
Substrates: -
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?
hexanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyhexanoyl-CoA + succinate + CO2
-
Substrates: -
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?
octadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyoctadecanoyl-CoA + succinate + CO2
-
Substrates: -
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octanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyoctanoyl-CoA + succinate + CO2
-
Substrates: -
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?
tetradecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxytetradecanoyl-CoA + succinate + CO2
-
Substrates: -
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?
3-methylhexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylhexadecanoyl-CoA + succinate + CO2
-
Substrates: -
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3-methylhexadecanoyl-CoA + 2-oxoglutarate + O2
2-hydroxy-3-methylhexadecanoyl-CoA + succinate + CO2
-
Substrates: -
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?
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
-
Substrates: -
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?
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
Substrates: -
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ir
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
Substrates: Refsums disease ia a neurological syndrome characterized by adult-onset retinitis pigmentosa, anosemia, sensory neuropathy and phytanic acidaemia. Many cases are caused by mutations in peroxidomal oxygenase phytanoyl-CoA 2-hydroxylase
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phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
-
Substrates: 3R and 3S epimers are hydroxylated with approximately equal efficiency. Both unprocessed proenzyme and mature form of PAHX are fully active
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phytanoyl-CoA + 2-oxoglutarate + O2
alpha-hydroxyphytanoyl-CoA + succinate + CO2
-
Substrates: -
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?
phytanoyl-CoA + 2-oxoglutarate + O2
alpha-hydroxyphytanoyl-CoA + succinate + CO2
-
Substrates: no activity with octadecanoyl-CoA, lignoceroyl-CoA, 2-methylhexadecanoyl-CoA and 4,8,12-trimethyltridecanoyl-CoA
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?
phytanoyl-CoA + 2-oxoglutarate + O2
alpha-hydroxyphytanoyl-CoA + succinate + CO2
-
Substrates: -
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?
additional information
?
-
-
Substrates: interaction between PAHX and the A2 domain of the coagulation factor VIII is a part responsible for the low-level expression of factor VIII
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?
additional information
?
-
-
Substrates: Resum disease might be characterized by an accumulation of not only phytanic acid but also ther 3-alkyl-branched fatty acids
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?
additional information
?
-
-
Substrates: no activity with isovaleryl-CoA, 4-phenyl-3-methylbutanoyl-CoA, 3-methylpentanoyl-CoA, hexadecanoyl-CoA, octanoyl-CoA, prostanoyl-CoA or 4-methylnonaoyl-CoA. Chain length of at least seven carbon atoms is a prerequisite for PAHX-dependent hydroxylation. The optimal chain length appears to be 9-12 carbon atoms. The branch at position 3 is a prerequisite for the activity of PAHX
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phytanoyl-CoA + 2-oxoglutarate + O2
2-hydroxyphytanoyl-CoA + succinate + CO2
Substrates: Refsums disease ia a neurological syndrome characterized by adult-onset retinitis pigmentosa, anosemia, sensory neuropathy and phytanic acidaemia. Many cases are caused by mutations in peroxidomal oxygenase phytanoyl-CoA 2-hydroxylase
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction between PAHX and the A2 domain of the coagulation factor VIII is a part responsible for the low-level expression of factor VIII
Products: -
Products: -
?
additional information
?
-
-
Substrates: Resum disease might be characterized by an accumulation of not only phytanic acid but also ther 3-alkyl-branched fatty acids
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
UTP, CTP, ITP, AMP, ADP, NAD+ and FAD can not act as cofactors, ATP and GTP can be replaced by adenosine-5'-O-(3-thiotriphosphate), adenylylimidodiphosphate, adenylyl-(beta,gamma-methylene)-diphosphonate and guanylyl-imidodiphosphate
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Iron
Fe2+ required. Maximal activity is 0.05-0.1 mM Fe2+ in absence of ATP
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
GTP
at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
additional information
-
not inhibited by bifonazole, clotrimazole, miconazole, ketoconazole
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
albumin
-
0.05 mM 3-methylhexadecanoyl-CoA, no hydroxylation in absence of albumin. Hydroxylation of 3-methylnonanoyl-CoA or 3-methyldodecanoyl-CoA is much less dependent on the presence of albumin
-
ATP
at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
GTP
at 0.1 mM Fe2+ 4 mM GTP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM GTP for 1.0 mM Fe2+
SCP-2
-
phytanoylis efficiently 2-hydroxylated by PAHX in vitro in the presence of mature SCO-2. SCP-2 increases discrimination between straight-chain and branched-chain substrates, i.e. it decreases activity with straight chain substrates and increase activity with branched-chain substrates. In vivo substrates for PAHX may be SCP-2 complexes
-
imidazole
at 0.1 mM Fe2+ 4 mM ATP inhibits enzyme activity. At increased Fe2+ concentrations ATP stimulates with a maximum at 64 mM ATP for 1.0 mM Fe2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adrenoleukodystrophy
Cerebro-hepato-renal (Zellweger) syndrome, adrenoleukodystrophy, and Refsum's disease: plasma changes and skin fibroblast phytanic acid oxidase.
Chondrodysplasia Punctata, Rhizomelic
Phytanoyl-CoA hydroxylase is not only deficient in classical Refsum disease but also in rhizomelic chondrodysplasia punctata.
Dementia
Genes associated with the progression of neurofibrillary tangles in Alzheimer's disease.
Lupus Nephritis
Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein.
Neoplasms
Identification of key genes in invasive clinically non-functioning pituitary adenoma by integrating analysis of DNA methylation and mRNA expression profiles.
Parkinson Disease
Genes associated with the progression of neurofibrillary tangles in Alzheimer's disease.
Peroxisomal Disorders
[Chondrodysplasia punctata (the Conradi-Hünermann syndrome). A clinical case report and review of the literature]
phytanoyl-coa dioxygenase deficiency
Dysmorphic syndrome with phytanic acid oxidase deficiency, abnormal very long chain fatty acids, and pipecolic acidemia: studies in four children.
phytanoyl-coa dioxygenase deficiency
Patterns of Refsum's disease. Phytanic acid oxidase deficiency.
phytanoyl-coa dioxygenase deficiency
Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease.
phytanoyl-coa dioxygenase deficiency
The Challenges of a Successful Pregnancy in a Patient with Adult Refsum's Disease due to Phytanoyl-CoA Hydroxylase Deficiency.
Refsum Disease
Cerebro-hepato-renal (Zellweger) syndrome, adrenoleukodystrophy, and Refsum's disease: plasma changes and skin fibroblast phytanic acid oxidase.
Refsum Disease
Characterization of phytanic acid omega-hydroxylation in human liver microsomes.
Refsum Disease
CYP4 isoform specificity in the omega-hydroxylation of phytanic acid, a potential route to elimination of the causative agent of Refsum's disease.
Refsum Disease
Dual-specificity tyrosine-phosphorylated and regulated kinase 1A (DYRK1A) interacts with the phytanoyl-CoA alpha-hydroxylase associated protein 1 (PAHX-AP1), a brain specific protein.
Refsum Disease
Dysmorphic syndrome with phytanic acid oxidase deficiency, abnormal very long chain fatty acids, and pipecolic acidemia: studies in four children.
Refsum Disease
Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease.
Refsum Disease
Identification of a brain specific protein that associates with a refsum disease gene product, phytanoyl-CoA alpha-hydroxylase.
Refsum Disease
Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein.
Refsum Disease
Infantile Refsum's disease (phytanic acid storage disease): a variant of Zellweger's syndrome?
Refsum Disease
Molecular basis of Refsum disease: identification of new mutations in the phytanoyl-CoA hydroxylase cDNA.
Refsum Disease
Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7).
Refsum Disease
Omega-hydroxylation of phytanic acid in rat liver microsomes: implications for Refsum disease.
Refsum Disease
Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease.
Refsum Disease
Phytanoyl-CoA hydroxylase is not only deficient in classical Refsum disease but also in rhizomelic chondrodysplasia punctata.
Refsum Disease
Restoration of phytanic acid oxidation in Refsum disease fibroblasts from patients with mutations in the phytanoyl-CoA hydroxylase gene.
Refsum Disease
Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.
Refsum Disease
Structure-function analysis of phytanoyl-CoA 2-hydroxylase mutations causing Refsum's disease.
Refsum Disease
The Challenges of a Successful Pregnancy in a Patient with Adult Refsum's Disease due to Phytanoyl-CoA Hydroxylase Deficiency.
Zellweger Syndrome
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 alpha-oxidation in humans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000001
-
in kidney cell line COS-1, activity can be induced 4fold by phytanic acid
0.0000018
-
in embryonic carcinoma cell line P19-EC, activity can be induced 4fold by phytanic acid
0.000002
-
in kidney cell line 293, activity can be induced 4fold by phytanic acid
0.000024
-
in hepatoma cell line FaO, activity can be induced 2.5fold by phytanic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
26 T4-like myoviruses, including 10 from non-cyanobacterial myoviruses and 16 from marine cyanobacterial myoviruses, isolated from Prochlorococcus sp. and Synechococcus sp.
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
phytanoyl-CoA dioxygenase domain-containing protein 1 plays an important role in egg shell formation of Bombyx mori
additional information
-
role of 2-oxoglutarate during cyanophage infection, overview
malfunction
infantile-onset Adult Refsum's disease due to phytanoyl-CoA hydroxylase ((PHYH) c.164delT, p.L55fsX12) mutation. The challenges of a successful pregnancy in a patient with Adult Refsums disease due to phytanoyl-CoA hydroxylase deficiency
malfunction
-
after knocking out the PHYHD1 by using CRISPR/Cas9, the chorion genes are significantly downregulated. The silencing of PHYHD1 leads to the downregulation of many chorion protein genes, thus directly causing giant eggs
Show AA Sequence and Transmembrane Helices (144 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35400
-
mature protein after cleavage of presumed leader sequence, calculation from cDNA sequence
41200
-
precursor protein with peroxisomal targeting signal type 2, calculation from cDNA sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
unprocessed proenzyme contains a N-terminal peroxisomal targeting sequence that is cleaved to give mature PAHX. Both forms are able to hydroxylate a range of CoA derivatives, but under the same assay conditions, the N-terminal Hexa-His-tagged unprocessed form is less active than the nontagged mature form
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method in 21% polyethylene glycol 3350, 0.3 M triammonium citrate, pH 7.1, at 18°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D177A
F275S
places a polar side chain in a hydrophobic pocket and possibly interferes with the overall structure or impair protein folding
G204S
H175A
H259A
mutation removes two of the hydrogen bonds and probably destabilizes the beta-turn, which in turn destabilizes the core double stranded beta-helix
N269H
N83Y
disruption of protein-protein interactions proposed to involve PAHX, such as that with sterol carrier protein-2, proposed to be responsible for solubilization and presentation of phytanoyl-CoA to PAHX
P29S
clinically observed mutant is fully active, mutation may result in a defective targeting of the protein to peroxisomes
Q176K
mutation causes partial uncoupling of 2-oxoglutarate conversion from phytanoyl-CoA oxidation
R245Q
disruption of protein-protein interactions proposed to involve PAHX, such as that with sterol carrier protein-2, proposed to be responsible for solubilization and presentation of phytanoyl-CoA to PAHX
R275Q
R275W
G204S
mutation causes partial uncoupling of 2-oxoglutarate conversion from phytanoyl-CoA oxidation
G204S
disruption of the 2-oxoglutarate binding pocket, uncouples 2-oxoglutarate and phytanoyl-CoA oxidation
N269H
mutation causes partial uncoupling of 2-oxoglutarate conversion from phytanoyl-CoA oxidation
N269H
disruption of the 2-oxoglutarate binding pocket, uncouples 2-oxoglutarate and phytanoyl-CoA oxidation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
carboxymethyl-Sepharose cation exchange chromatography and Superdex S75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
T4-like cyanopohage, marine cyanobacterial and non-cyanobacterial, genotyping, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
diagnostics
assays for Refsums disease should not be based on PAHX activity alone. At least four different types of mutation cause loss of PAHX activity in vivo. Mutations to the peroxisomal targeting sequence do not affect catalytic function but probably affect targeting or degradation of the enzyme. A second group of mutations, including truncation and missense mutations, results in total loss of activity. A third group of mutations results in uncoupling of substrate oxidation from that of 2-oxoglutarate. A fourth group of mutations causes partial inactivation by hindering binding/utilization of the 2-oxoglutarate cosubstrate and/or iron(II) cofactor. From the therapeutic and biochemical view-point the latter two groups are particularly interesting since it may be possible to restore their activity with modified cosubstrates
diagnostics
-
the substrate phytanoyl-CoA is difficult to handle because of its amphipathic properties. Commercially available alternative substrates, such as hexadecanoyl-CoA or isovaleryl-CoA are potentially usefull
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mihalik, S.J.; Rainville, A.M.; Watkins, P.A.
Phytanic acid oxidation in rat liver peroxisomes. Production of alpha-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors
Eur. J. Biochem.
232
545-551
1995
Rattus norvegicus
brenda
Jansen, G.A.; Mihalik, S.J.; Watkins, P.A.; Moser, H.W.; Jakobs, C.; Denis, C.; Wanders, R.J.A.
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 alpha-oxidation in humans
Biochem. Biophys. Res. Commun.
229
205-210
1996
Homo sapiens
brenda
Mihalik, S.J.; Morrell, J.C.; Kim, D.; Sacksteder, K.A.; Watkins, P.A.; Gould, S.J.
Identification of PAHX, a Refsum disease gene
Nature Genet.
17
185-189
1997
Homo sapiens
brenda
Jansen, G.A.; Mihalik, S.J.; Watkins, P.A.; Jakobs, C.; Moser, H.W.; Wanders, R.J.A.
Characterization of phytanoyl-Coenzyme A hydroxylase in human liver and activity measurements in patients with peroxisomal disorders
Clin. Chim. Acta
271
203-211
1998
Homo sapiens
brenda
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.; Wanders, R.J.A.
Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene
Nature Genet.
17
190-193
1997
Homo sapiens, Rattus norvegicus
brenda
Chahal, A.; Khan, M.; Pai, S.G.; Barbosa, E.; Singh, I.
Restoration of phytanic acid oxidation in Refsum disease fibroblasts from patients with mutations in the phytanoyl-CoA hydroxylase gene
FEBS Lett.
429
119-122
1998
Homo sapiens
brenda
Jansen, G.A.; Ferdinandusse, S.; Hogenhout, E.M.; Verhoeven, N.M.; Jakobs, C.; Wanders, R.J.A.
Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease
Adv. Exp. Med. Biol.
466
371-376
1999
Homo sapiens
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Homo sapiens, Mus musculus, Platyrrhini, Rattus norvegicus
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Homo sapiens, Rattus norvegicus
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Homo sapiens
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Homo sapiens
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Mukherji, M.; Chien, W.; Kershaw, N.J.; Clifton, I.J.; Schofield, C.J.; Wierzbicki, A.S.; Lloyd, M.D.
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Hum. Mol. Genet.
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1971-1982
2001
Homo sapiens (O14832)
brenda
Chen, C.; Wang, Q.; Fang, X.; Xu, Q.; Chi, C.; Gu, J.
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Homo sapiens
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Foulon, V.; Asselberghs, S.; Geens, W.; Mannaerts, G.P.; Casteels, M.; van Veldhoven, P.P.
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Homo sapiens
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Searls, T.; Butler, D.; Chien, W.; Mukherji, M.; Lloyd, M.D.; Schofield, C.J.