Institut for Plante- og Miljøvidenskab > Ansatte
1871 Frb. C
Assistant Professor for Metabolic Engineering and Head of Metabolomics platform at DynaMo - Center of Excellence for Dynamic Molecular Interactions
Cross-talk between primary and specialized metabolism on the example of aliphatic glucosinolates and the biosynthesis of the amino acid methionine in the model system Arabidopsis thaliana. Major techniques applied include targeted and untargeted LC-MS analysis and confocal laser scanning microscopy (CLSM).
Elucidation and alleviation of bottle necks in metabolic engineering of (aliphatic) glucosinolates to facilitate transfer of the complex pathway into a microbial production host (E.coli and yeast). Main techniques include transient expression in Nicotiana benthamiana and development of a plasmid-based expression system for complex pathways in E.coli.
Methionine chain elongation in aliphatic glucosinolate biosynthesis
Aliphatic glucosinolates represent a special group within glucosinolates which are formed from chain-elongated methionine. This stands in contrast to the biosynthesis of indolyl- or benzylglucosinolates where unmodified amino acids (i.e. tryptophane or phenylalanine) are the initial substrates.
The process of methionine chain elongation demands for an extra machinery which is mostly localized in plastids with one cytosolic and three plastidal enzymes.
The plastidal steps of methionine chain elongation were found to have evolved from leucine biosynthesis ( Field et al. 2004; Textor et al., 2004; Schuster et al., 2006; Binder et al., 2007; He et al., 2010; De Kraker et al., 2011). Moreover, the large subunit of isopropylmalate-isomerase is employed by both pathways. The large subunit forms heterodimers with one of three different small subunits of either pathway. These small subunits were found to be responsible for substrate specificity of the catalyzed reactions.
Questions that are currently addressed using the model plant Arabidopsis thaliana :
- Dynamics of methionine chain elongation
- Protein-protein interactions between biosynthetic enzymes within methionine chain elongation as well as with leucine biosynthesis
- Metabolic engineering of methionine chain elongation into a microbial host