Fig. 1. Lysine metabolic pathways.

Fig. 2. Nucleotide and predicted amino acid sequences of human AADAT. Nucleotides are numbered starting with +1 at the predicted initiation codon (ATG). The deduced amino acid sequence is shown in single-letter code below the nucleotide sequence. The predicted mitochondrial cleavage signal is boxed. The residues involved in cofactor binding are shaded and the lysine reisdue information in the formation of an aldimine bond with pyridoxal 5^′-phosphate (PLP) is indicated in bold [25].

Fig. 3. Sequence alignment of human AADAT (Hs AADAT), mouse KAT2 (Mm Kat2), rat KAT2 (Rn Kat2), and S. pombe aromatic aminotransferase I (ARO8) proteins. Residues that are identical (dark gray) or similar (light gray) are shown. The lysine residue that forms the aldimine bond with PLP is indicated by a star. The residues involved in cofactor binding are indicated by arrowheads [22].

Fig. 4. (A) Genomic structure of AADAT. Vertical lines and numbers indicate exons. Horizontal lines between exons represent introns. The relative sizes of each exon and intron are drawn to scale. (B) Intron–exon boundaries of AADAT genomic DNA. Exon and intron sequences are represented by upper and lower cases, respectively. The sizes of the exons were determined by sequencing.

Fig. 5. FISH. Metaphase cell showing FISH of BAC clone RP11-25G11 (red signals).

Fig. 6. Northern blot analysis. Mouse multiple tissue Northern blots were hybridized with a [α-³²P] labeled probe (full-length ORF). Numbers on the left represent standard molecular weight markers.

Fig. 7. AADAT enzyme assay. pMBP=vector alone; pMPB + AADAT=vector with a full length ORF insert.