Article
Substitutions of coenzyme-binding, nonpolar residues improve the low-temperature activity of thermophilic dehydrogenases.
Biochemistry - 11 Oct 2011
Hayashi Sayaka, Akanuma Satoshi, Onuki Wakana, Tokunaga Chihiro, Yamagishi Akihiko
Abstract excerpt
Although enzymes of thermophilic organisms are often very resistant to thermal denaturation, they are usually less active than their mesophilic or psychrophilic homologues at moderate or low temperatures. To explore the structural features that would improve the activity of a thermophilic enzyme at less than optimal temperatures, we randomly mutated the DNA of single-site mutants of the thermostable Thermus...
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