1. Supplemental Figure S2. Sequence comparison of the Arabidopsis homologue of PAHX with human PHYD1 (phytanoyl-CoA dioxygenase domain containing 1) and human PAHX. AtPAHX, thale cress Arabidopsis thaliana (At2g01490), HsPHYD1, human Homo sapiens (AAH ), HsPAHX, human Homo sapiens (AAB ). The residues in black indicate amino acids that are identical to those of Arabidopsis PAHX in the alignment, and those in gray indicate similar amino acids to those of Arabidopsis PAHX. The enzyme phytanoyl-CoA 2-hydroxylase (PAHX/PhyH) belongs to the family of 2-oxoglutarate (2OG)-dependent oxygenases (Mihalik et al., 1995). The red triangles indicate conserved amino acid residues for Fe(II) and 2-oxoglutalate-binding (including His175, Asp177, Trp193, Glu197, Gly204, His264, Arg275, and Ser266) together with other active residues (e.g. His281) in HsPAHX that were resolved by the structural study (McDonough et al., 2005). Alignment was performed using ClustalW ( Boxshading was produced by BOXSHADE 3.21 (
Supplementary references:
McDonough MA, Kavanagh KL, Butler D, Searls T, Oppermann U, Schofield CJ (2005) Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum Disease. J. Biol. Chem. 280:
Mihalik SJ, Rainville AM, Watkins PA (1995) Phytanic acid a- oxidation in rat liver peroxisomes. Production of a-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem 232: