Prof. Dr. Kai Tittmann
Professor of Molecular Enzymology
Major Research Interests
The central research topic of our department is the analysis of molecular reaction mechanisms of enzymes as nature's chemical catalysts. In this context, we study enzymes with vitamin-derived cofactors, with metal ions, and Schiff base-forming enzymes. A particular focus is laid on the structural and kinetic characterization of enzymatic reaction intermediates by high-resolution X-ray crystallography, steady-state and transient kinetic methods, NMR spectroscopy and theoretical studies. Knowledge about the reaction mechanism is exploited to redesign enzymes for biocatalytic applications and for drug design.
Homepage Department/Research Group:
Selected Recent Publications
Sub-Angström resolution crystallography reveals physical distortions that enhance
reactivity of a covalent enzymatic intermediate. Nature Chem 5: 762?767
Observation of a stable carbene at the active site of a thiamin enzyme.
Nature Chem Biol 9: 488-490
Unexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase
highlight unrecognized chemical versatility of the thiamin cofactor. Proc Natl Acad Sci USA 109(27): 10867-72
K (2011) Twisted Schiff-base Intermediates and Substrate Locale Revise
Transaldolase Mechanism. Nature Chem Biol 7: 678-684
pyruvate decarboxylase into an enantioselective carboligase with biosynthetic
potential. J Am Chem Soc 133: 3609-3616
K, Shaanan B (2008) Glyoxylate carboligase challenges the paradigm for
activation of thiamin-dependent enzymes. Nature Chem Biol 4: 113-118
cycle of a thiamin diphosphate enzyme examined by cryocrystallography.
Nature Chem Biol 2: 324-328