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Title: Identification of a novel glyoxylate reductase supports phylogeny-based enzymatic substrate specificity prediction
Authors: Fauvart, Maarten
Braeken, Kristien
Daniels, Ruth
Vos, Karen
Ndayizeye, Maxime
Noben, Jean-Paul
Robben, Johan
Vanderleyden, Jozef
Michiels, Jan # ×
Issue Date: Sep-2007
Publisher: Elsevier
Series Title: Biochimica et Biophysica Acta. Proteins and Proteomics vol:1774 issue:9 pages:1092-1098
Abstract: Phylogenetic analysis of the superfamily of D-2-hydroxyacid dehydrogenases identified the previously unrecognized cluster of glyoxylate/hydroxypyruvate reductases (GHPR). Based on the genome sequence of Rhizobium etli, the nodulating endosymbiont of the common bean plant, we predicted a putative 3-phosphoglycerate dehydrogenase to exhibit GHPR activity instead. The protein was overexpressed and purified. The enzyme is homodimeric under native conditions and is indeed capable of reducing both glyoxylate and hydroxypyruvate. Other substrates are phenylpyruvate and ketobutyrate. The highest activity was observed with glyoxylate and phenylpyruvate, both having approximately the same k(cat)/K(m) ratio. This kind of substrate specificity has not been reported previously for a GHPR. The optimal pH for the reduction of phenylpyruvate to phenyllactate is pH 7. These data lend support to the idea of predicting enzymatic substrate specificity based on phylogenetic clustering.
URI: 
ISSN: 1570-9639
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre of Microbial and Plant Genetics
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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