Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

Phyh - phytanoyl-CoA 2-hydroxylase

Rattus norvegicus

Synonyms: PhyH, Phytanic acid oxidase, Phytanoyl-CoA alpha-hydroxylase, Phytanoyl-CoA dioxygenase, peroxisomal

Xu, F. et al., Jansen, G.A. et al., Skjeldal, O.H. et al., Jansen, G.A. et al., Jansen, G.A. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Phyh

Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene [1].

High impact information on Phyh

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 [1].
Phytanoyl-CoA hydroxylase (PhyH) catalyzes the conversion of phytanoyl-CoA to 2-hydroxyphytanoyl-CoA, which is the first step in the phytanic acid alpha-oxidation pathway [2].
However, individuals with Refsum's disease are genetically deficient in the required phytanoyl-CoA alpha-hydroxylase and suffer from neurological pathologies caused by the accumulation of phytanic acid [3].
The first step occurs in peroxisomes and is catalysed by phytanoyl-CoA hydroxylase [4].
A series of experiments preformed to localize the phytanic acid oxidase in subcellular fractions of rat liver show, however, that the alpha-oxidation of phytanic acid is a mitochondrial process [5].

References

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]
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]
CYP4 isoform specificity in the omega-hydroxylation of phytanic acid, a potential route to elimination of the causative agent of Refsum's disease. Xu, F., Ng, V.Y., Kroetz, D.L., de Montellano, P.R. J. Pharmacol. Exp. Ther. (2006) [Pubmed]
Phytanic acid alpha-oxidation: identification of 2-hydroxyphytanoyl-CoA lyase in rat liver and its localisation in peroxisomes. Jansen, G.A., Verhoeven, N.M., Denis, S., Romeijn, G., Jakobs, C., ten Brink, H.J., Wanders, R.J. Biochim. Biophys. Acta (1999) [Pubmed]
The subcellular localization of phytanic acid oxidase in rat liver. Skjeldal, O.H., Stokke, O. Biochim. Biophys. Acta (1987) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

LOC100300115	Bos taurus
PHYH	Bos taurus
CELE_ZK550.6	Caenorhabditis elegans
LOC478001	Canis lupus familiaris
LOC478000	Canis lupus familiaris
phyh	Danio rerio
LOC798210	Danio rerio
PHYH	Gallus gallus
PHYH	Homo sapiens
PHYH	Macaca mulatta
Phyh	Mus musculus
PHYH	Pan troglodytes
phyh	Xenopus (Silurana) tropicalis

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.