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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/4100

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, Jos
Michiels, Jan
Issue Date: 2007
Publisher: ELSEVIER SCIENCE BV
Citation: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1774(9). p. 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. (c) 2007 Elsevier B.V. All rights reserved.
Notes: Katholieke Univ Leuven, Ctr Microbial & Plant Genet, B-3001 Heverlee, Belgium. Univ Hasselt, Biomed Onderzoek Inst, B-3590 Diepenbeek, Belgium.MICHIELS, J, Katholieke Univ Leuven, Ctr Microbial & Plant Genet, Kasteelpk Arenberg 20, B-3001 Heverlee, Belgium.jan.michiels@biw.kuleuven.be
URI: http://hdl.handle.net/1942/4100
DOI: 10.1016/j.bbapap.2007.06.009
ISI #: 000249840000003
ISSN: 1570-9639
Category: A1
Type: Journal Contribution
Validation: ecoom, 2008
Appears in Collections: Research publications

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