Abstract
Publisher Summary Dihydrofolate reductase (DHFR) plays a central role in the metabolism of both prokaryotes and eukaryotes. It catalyzes the NADPHdependent reduction of dihydrofolic acid (DHF) to tetrahydrofolic acid (THF), thereby restoring an important cofactor in one-carbon transfer reactions. The enzyme has been widely studied both structurally and mechanistically. Among the more than 40 DHFRs characterized so far, the enzyme from the hyperthermophilic bacterium Thermotoga maritima (Tm DHFR) exhibits the highest intrinsic stability with the exceptional additional characteristic of forming a tightly associated homodimer. Tm DHFR may serve as a model system for structural and mechanistical comparisons with its mesophilic counterparts. As a dimer, it promises insight into mechanisms of thermophilic adaptation at all levels of the structural hierarchy of globular proteins. In this context, the extreme stability offers experimental advantages. However, there are difficulties in handling the enzyme, which are discussed in this chapter.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
