Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous
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A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.
Key wordsPLP-dependent decarboxylase Evolution Profile analysis
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- Siegel G, Agranoff B, Albers RW, Molinoff P (1989) Basic neurochemistry, ed 4. Raven Press, New YorkGoogle Scholar
- Tanaka T, Horio Y, Taketoshi M, Imamura I, Ando-Yamamoto M, Kangawa K, Matsuo H, Kuroda M, Wada H (1989) Molecular cloning and sequencing of a cDNA of rat dopa decarboxylase: partial amino acid homologies with other enzymes synthesizing catecholamines. Proc Natl Acad Sci USA 86: 8142–8146PubMedGoogle Scholar