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Supplementary references:

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  1. Supplemental Figure S3. Sequence comparison of the Arabidopsis homologue of 2-HPCL and human 2-HPCL. AtHPCL, thale cress Arabidopsis thaliana (At5g17380), HsHPCL, human Homo sapiens (Q9UJ83). 2-hydroxyphytanoyl-CoA lyase is a thiamine pyrophosphate (TPP)-dependent enzyme that catalyzes the carbon-carbon bond cleavage during α-oxidation of 3-methyl-branched fatty acids (Foulon et al. 1999). The blue box near the N-terminus indicates a pyrimidine (PYR) binding domain (cd07035) of pyruvate oxidase and related proteins. The PYR domain is found in many key metabolic enzymes which use thiamine pyrophosphate (TPP) as a cofactor. The red box near the C-terminus indicates a conserved domain of BZL_OCoD_HPCL subfamily (cd02004), composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). The domain structure was annotated using the conserved domain database (Marchler-Bauer et al., 2009). Pairwise alignment was performed using ClustaW (http://www.ebi.ac.uk/clustalw/). Boxshading was produced by BOXSHADE 3.21 (http://ch.embnet.org/software/BOX_form.html).

  2. Supplementary references: Foulon V, Antonenkov VD, Croes K, Waelkens E, Mannaerts GP, Van Veldhoven PP. and Casteels M (1999) Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during α-oxidation of 3-methyl-branched fatty acids.Proc Natl Acad Sci USA 96: 10039-10044 Marchler-Bauer A, Anderson JB, Chitsaz F, Derbyshire MK, DeWeese-Scott C, Fong JH, Geer LY, Geer RC, Gonzales NR, Gwadz M, He S, Hurwitz DI, Jackson JD, Ke Z, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Tasneem A, Thanki N, Yamashita RA, Zhang D, Zhang N, and Bryant SH. (2009) CDD: specific functional annotation with the Conserved Domain Database. Nucleic Acids Res. 37: D205-210

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