2015 journal article
Discovery of a novel amino acid racemase through exploration of natural variation in Arabidopsis thaliana
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 112(37), 11726–11731.
author keywords: D-amino acid; racemase; genome-wide association; secondary metabolism; natural variation
MeSH headings : Amino Acid Isomerases / genetics; Amino Acid Isomerases / physiology; Arabidopsis / enzymology; Arabidopsis / genetics; Arabidopsis Proteins / genetics; Arabidopsis Proteins / physiology; Chromatography, High Pressure Liquid; Chromatography, Liquid; Chromosome Mapping; Gene Expression Regulation, Plant; Genetic Variation; Genome-Wide Association Study; Genomics; Genotype; Isoleucine / analogs & derivatives; Isoleucine / chemistry; Mass Spectrometry; Metabolomics; Mutation; Quantitative Trait Loci; Stereoisomerism
TL;DR:
This finding provides the first functional characterization of a eukaryotic member of a large and widely conserved phenazine biosynthesis protein PhzF-like protein family, and demonstrates that exploitation of natural metabolic variation by integrating metabolomics with genome-wide association is a powerful approach for functional genomics study of specialized metabolism.
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open access via www.pnas.org (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
12. Responsible Consumption and Production
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
Significance We describe how untargeted metabolic profiling and genome-wide association analysis was used in Arabidopsis thaliana to link natural products (secondary metabolites) with genes controlling their production. This powerful approach exposed metabolite–enzyme connections even without prior knowledge of the metabolite identity or the biochemical function of the associated enzyme. Further chemical and genetic analysis synergistically led to the discovery and characterization of a d -amino acid derivative, N -malonyl- d -allo-isoleucine, and a novel amino acid racemase responsible for its biosynthesis. Little is known about d -amino acid metabolism and its natural variation in plants. Additionally, this is the first functional characterization of a eukaryotic member of a large family of phenazine biosynthesis protein phzF-like proteins conserved across all the kingdoms.