Subunit structure of 3,4-dihydroxyphenylalanine decarboxylase from pig kidney

Molecular mechanism of PdxR – a transcriptional activator involved in the regulation of vitamin B6 biosynthesis in the probiotic bacterium Bacillus clausii

“…The band at 335 nm arguably corresponds to the enolimine form of the same Schiff base, as indicated by the presence of emission bands at 400 and 500 nm when the protein was excited at 335 nm (data not shown) [24] and similarly to GabR from B. subtilis [25]. Treating the protein with hydroxylamine [26], we could obtain an apo-form of PdxR, in which the bands at 335 and 425 nm had disappeared (Fig. 4A).…”

Recent Topics in Pyridoxal 5'-Phosphate Enzyme Studies

“…1.28) (AroDC) is a relatively nonspecific enzyme catalyzing decarboxylation of phenylalanine, tryptophan, and their hydroxylated derivatives (156), and is important for the formation of biogenic amines. AroDC purified from rat liver (157,158) or pig kidney (159,160) shows absorption maxima at 330 nm and 420 nm, characteristic of PLP-enzymes. The intensity ratios of the two peaks, E33o!E420, is 2.0-2.7 and considerably larger than that (about 0.5) of Morganella histidine de carboxylase, another PLP-dependent decarboxylase (168).…”

DDC (dopa decarboxylase (aromatic L-amino acid decarboxylase))

“…The full-length protein molecule consists of 480 amino acids (Ichinose et al, 1989). DDC is a pyridoxal-5-phosphate (PLP)dependent enzyme possessing a single binding-site for PLP per subunit (Voltattorni et al, 1982;Ichinose et al, 1989;Burkhard et al, 2001). Expression of the DDC gene, in humans, results in the production of additional protein isoforms (O'Malley et al, 1995;Chang et al, 1996;Vassilacopoulou et al, 2004).…”