Many of the proteins of the CCM of T. tenax (about 22; partly in collaboration with R. Hensel) and other hyperthermophiles, either identified by classical reversed genetics or new genomics-based methods, were expressed in Escherichia coli, purified and the predicted activity was confirmed by enzymatic studies [6-10, 13, 17, 20, 23, 25, 26].

Fructose-1,6-bisphosphate aldolase (archaeal type, Class I) Thermoproteus tenax [12, 14, 16, 19].

These detailed biochemical and molecular genetic studies aim at the understanding of the regulation of proteins and pathways on protein as well as gene level. The objective is to unravel their physiological role and their integration in cellular networks. In addition to functional studies, also phylogenetic aspects (collaboration with H. Brinkmann) as well as the resolution of protein structures and reaction mechanisms (collaboration with E. Pohl) play an important role in our studies. Our approach has proven successful, for example, in the investigation of archaeal type Class I fructose1,6-bisphosphate aldolase [12, 14, 16, 19] and KD(P)G aldolase [20, 27].