Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic Archaeon, ES4.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference51 articles.
1. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya.
2. Hyperthermophilic microorganisms
3. Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus
4. Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation.
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1. Genetic Examination of Initial Amino Acid Oxidation and Glutamate Catabolism in the Hyperthermophilic Archaeon Thermococcus kodakarensis;Journal of Bacteriology;2013-05
2. Insights into Thermal Stability from a Comparison of the Glutamate Dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis;European Journal of Biochemistry;2008-06-28
3. The First Crystal Structure of Hyperthermostable NAD-dependent Glutamate Dehydrogenase from Pyrobaculum islandicum;Journal of Molecular Biology;2005-01
4. Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds;European Journal of Biochemistry;2004-12
5. α-Amylases and amylopullulanase from Pyrococcus furiosus;Methods in Enzymology;2001
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