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.
Bioscience, Biotechnology, and Biochemistry
Volume 76, 2012 - Issue 9
![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related Research Data
In Vitro Heat Effect on Functional and Conformational Changes of Cyclodextrin Glucanotransferase from Hyperthermophilic Archaea
Source:
Elsevier BV
Thermostable amino acid dehydrogenases: applications and gene cloning
Source:
Elsevier BV
Di-myo-inositol-1,1'-phosphate: a new inositol phosphate isolated from Pyrococcus woesei.
Source:
Wiley
CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
Source:
International Union of Crystallography (IUCr)
Amino Acid Dehydrogenases and TheirApplications
Source:
CRC Press
In vitro heat effect on heterooligomeric subunit assembly of thermostable indolepyruvate ferredoxin oxidoreductase
Source:
Federation of European Biochemical Societies. Published by Elsevier B.V.
Purification and characterization of extremely thermo-stable glutamate dehydrogenase from a hyperthermophilic archaeon Thermococcus litoralis.
Source:
Informa UK Limited
Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus.
Source:
Oxford University Press (OUP)
Chapter 6 Structure analysis by small-angle X-ray scattering
Source:
Elsevier
Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing.
Source:
The Biophysical Society. Published by Elsevier Inc.
Linking provided by
