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Abstract
This study demonstrates that Escherichia coli glutamate decarboxylase (EcGadB) effectively decarboxylates the L-isomer of D,L-2-amino-4-(hydroxyphosphinyl)butyric acid (D,L-Glu-γ-PH), a phosphinic analog of glutamate, yielding 3-aminopropylphosphinic acid (GABA-PH). The research further shows that GABA-PH is metabolized by GABase to 3-(hydroxyphosphinyl)propionic acid (Succinate-PH). These findings suggest that the phosphinic group is a bioisostere of the carboxyl group, opening possibilities for prodrug design.
Publisher
Communications Chemistry
Published On
Sep 02, 2020
Authors
Daniela De Biase, Francesca Cappadocio, Eugenia Pennacchietti, Fabio Giovannercole, Antonio Coluccia, Jouko Vepsäläinen, Alex Khomutov
Tags
Escherichia coli
glutamate decarboxylase
phosphinic acid
metabolites
prodrug design
bioisostere
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