Transaminases are established tools for the asymmetric synthesis of chiral primary amines and amino acids. Our research aims to understand how the catalytic properties of amine transaminases are controlled by the amino acid composition of the enzymes’ active sites. This talk will summarize our knowledge of structure-function relationships and how stereo preference and activity level towards model substrates can be predicted from sequence alignments. We found that the hydrophobicity of active site residues is important for the level of activity. For the application of transaminases, an important aspect is their stability. Although thermostable enzymes were discovered that can be stored at higher temperatures for prolonged times, stability while doing catalysis under process conditions is the more challenging requirement. The role of the oligomerization state for stability under operational and resting conditions will be discussed.
Matthias Höhne is a Professor at the Technical University of Berlin. He studied biochemistry at the Ernst Moritz Arndt University of Greifswald and in 2009 he received his PhD there with a thesis on the synthesis of optically active amines with ω-transaminases. Subsequently, he was a postdoctoral researcher at the University of Heidelberg until 2011, conducting research in organic chemistry on the selection of enantioselective iridium-DNA hybrid catalysts. From 2012 to 2018, he was a junior professor at the Ernst Moritz Arndt University of Greifswald and subsequently a junior research group leader there. In 2018, he received an ERC Starting Grant. Since 2023 he continues with his research team at Technical University of Berlin.
