Premium
Peroxisomal trans ‐2‐enoyl‐CoA reductase is involved in phytol degradation
Author(s) -
Gloerich J.,
Ruiter J.P.N.,
van den Brink D.M.,
Ofman R.,
Ferdinandusse S.,
Wanders R.J.A.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.011
Subject(s) - phytanic acid , phytol , peroxisome , reductase , biochemistry , chemistry , enzyme , coenzyme a , stereochemistry , receptor
Phytol is a naturally occurring precursor of phytanic acid. The last step in the conversion of phytol to phytanoyl‐CoA is the reduction of phytenoyl‐CoA mediated by an, as yet, unidentified enzyme. A candidate for this reaction is a previously described peroxisomal trans ‐2‐enoyl‐CoA reductase (TER). To investigate this, human TER was expressed in E. coli as an MBP‐fusion protein. The purified recombinant protein was shown to have high reductase activity towards trans ‐phytenoyl‐CoA, but not towards the peroxisomal β‐oxidation intermediates C24:1‐CoA and pristenoyl‐CoA. In conclusion, our results show that human TER is responsible for the reduction of phytenoyl‐CoA to phytanoyl‐CoA in peroxisomes.