Related Experiment Video
Updated: May 18, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Structural characteristics of active and inactive glutamate dehydrogenases from the hyperthermophile Pyrobaculum
1Microbial Genetics Division, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan. ohshima@agr.kyushu-u.ac.jp
Abstract:
The enzymes from hyperthermophiles are generally extremely thermostable and lose little or no activity during long periods under a variety conditions. This high stability is very attractive, in that it gives the enzymes potential for use in numerous bioprocesses. My research group has investigated this high stability from the viewpoint of the relationship between function and structure. In this review, I describe the molecular mechanism underlying the extreme stability of unboiled NAD-dependent glutamate dehydrogenase from the hyperthermophile Pyrobaculum islandicum. I also describe the activation of the inactive recombinant enzyme produced in mesophilic Escherichia coli from the viewpoint of the relationship between structure and activity.
Related Concept Videos
Diversity of Archaea IV
Hyperthermophilic Bacteria
Diversity of Archaea III
Diversity of Archaea I
Anoxygenic Phototrophic Bacteria
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

