Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous

52Citations
Citations of this article
12Readers
Mendeley users who have this article in their library.
Get full text

Abstract

A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila 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. © 1990 Springer-Verlag New York Inc.

Cite

CITATION STYLE

APA

Jackson, F. R. (1990, October). Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous. Journal of Molecular Evolution. Springer-Verlag. https://doi.org/10.1007/BF02101126

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free