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Biochemical and structural characterization of two new families of Transaldolases


Transaldolases (Tal) catalyse the reversible transfer of an activated dihydroxyacetone moiety from a donor ketose to an acceptor aldose. As they catalyse the formation of two adjacent chiral carbon atoms with strict stereo specificity they are desired tool s in asymmetric synthesis but their use is limited due to their substrate specificity. So approaches are taken to understand and modify the substrate and stereo specificity of transaldolases. To find transaldolases with new properties we made use of the in creasing number of sequences available and discovered two new families of large transaldolases. One family consists of cyanobacterial sequences and the other one of plant sequences. Representatives of both families will be studied with respect to their sub strate and stereo specificity and compared to Tal B from Escherichia coli. Furthermore their three dimensional structure will be determined by X-ray crystallography. The cyanobacterial Tals which contain additional EF-hand motifs will be investigated for t heir capacity to bind Ca2+ and its possible regulatory function. After a training period abroad (3 years as a Ph.D. student at the Eidgenössische Technische Hochschule (ETH) Zürich, Switzerland and 2 years initial Marie Curie Individual Fellowship at the University of Cambridge, UK) Anne Samland is now coming back to her home country Germany. Besides the project proposed here she will be involved in on-going research in the field of C-C bond forming enzymes and their biotechnological application. A new proteomic group for the University will be set up in the institute. She will be responsible as a specialist for protein chromatography and MALDI-TOF mass spectrometry. She will be part of the teaching staff and as such will be supervising students in practical courses and will be involved in lecturing. This will give her the opportunity for re-integration into the German system.

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