The Enzyme Database

Your query returned 4 entries.    printer_iconPrintable version

Accepted name: hydroxyphytanate oxidase
Reaction: L-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2
Other name(s): L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Systematic name: L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114454-12-5
1.  Vamecq, J. and Draye, J.P. The enzymatic and mass spectrometric identification of 2-oxophytanic acid, a product of the peroxisomal oxidation of l-2-hydroxyphytanic acid. Biomed. Environ. Mass Spectrom. 15 (1988) 345–351. [DOI] [PMID: 3288289]
[EC created 1990]
Accepted name: phytanoyl-CoA dioxygenase
Reaction: phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Glossary: phytanate = 3,7,11,15-tetramethylhexadecanoate
Other name(s): phytanoyl-CoA hydroxylase
Systematic name: phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Part of the peroxisomal phytanic acid α-oxidation pathway. Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 185402-46-4
1.  Jansen, G.A., Mihalik, S.J., Watkins, P.A., Jakobs, C., Moser, H.W. and Wanders, R.J.A. Characterization of phytanoyl-CoA hydroxylase in human liver and activity measurements in patients with peroxisomal disorders. Clin. Chim. Acta 271 (1998) 203–211. [DOI] [PMID: 9565335]
2.  Jansen, G.A., Mihalik, S.J., Watkins, P.A., Moser, H.W., Jakobs, C., Denis, S. and 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 α-oxidation in humans. Biochem. Biophys. Res. Commun. 229 (1996) 205–210. [DOI] [PMID: 8954107]
3.  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. and Wanders, R.J.A. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat. Genet. 17 (1997) 190–193. [DOI] [PMID: 9326940]
4.  Mihalik, S.J., Rainville, A.M. and Watkins, P.A. Phytanic acid α-oxidation in rat liver peroxisomes. Production of α-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem. 232 (1995) 545–551. [DOI] [PMID: 7556205]
5.  Mihalik, S.J., Morrell, J.C., Kim, D., Sacksteder, K.A., Watkins, P.A. and Gould, S.J. Identification of PAHX, a Refsum disease gene. Nat. Genet. 17 (1997) 185–189. [DOI] [PMID: 9326939]
[EC created 2000]
Accepted name: methyl-branched lipid ω-hydroxylase
Reaction: a methyl-branched lipid + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = an ω-hydroxy-methyl-branched lipid + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
Other name(s): CYP124
Systematic name: methyl-branched lipid,reduced-ferredoxin:oxygen oxidoreductase (ω-hydroxylating)
Comments: The enzyme, found in pathogenic and nonpathogenic mycobacteria species, actinomycetes, and some proteobacteria, hydroxylates the ω-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate. It is a P-450 heme-thiolate enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Johnston, J.B., Kells, P.M., Podust, L.M. and Ortiz de Montellano, P.R. Biochemical and structural characterization of CYP124: a methyl-branched lipid ω-hydroxylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 106 (2009) 20687–20692. [DOI] [PMID: 19933331]
[EC created 2015]
Accepted name: phytanate—CoA ligase
Reaction: ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA
Other name(s): phytanoyl-CoA ligase
Systematic name: phytanate:CoA ligase (AMP-forming)
Comments: Not identical with EC long-chain-fatty-acid—[acyl-carrier-protein] ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 105238-50-4
1.  Muralidharan, F.N. and Muralidharan, V.B. Phytanoyl-CoA ligase activity in rat liver. Biochem. Int. 13 (1986) 123–130. [PMID: 3753503]
[EC created 1989]

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