InterPro domain: IPR010977

A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group [ 1 , 2 ]. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase), which catalyses the decarboxylation of tryptophan to tryptamine [ 3 ]; tyrosine decarboxylase, whichconverts tyrosine into tyramine; and histidine decarboxylase, which catalyses the decarboxylation of histidine to histamine [ 4 ]. These enzymes belong to the group II decarboxylases [ 5 , 5 ].

1. Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221, 997-1002
2. Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous. J. Mol. Evol. 31, 325-9
3. Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. J. Biochem. 120, 369-76
4. Characterization and expression of the complementary DNA encoding rat histidine decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 87, 733-7