Molecular and Comparative Analysis of the HyperthermostablePyrococcus FuriosusGlutamate Dehydrogenase and its Gene
Author:
Affiliation:
1. Department of Microbiology, Wageningen Agricultural University, Hesselink van Suchtelenweg 4, 6703 CT, Wageningen, The Netherlands
2. Swiss Federal Institute for Environmental Science and Technology (EAWAG), CH-8600, Dubendorf, Switzerland
Publisher
Informa UK Limited
Subject
General Agricultural and Biological Sciences,Biochemistry,Biotechnology,Catalysis
Link
https://www.tandfonline.com/doi/pdf/10.3109/10242429409034383
Reference43 articles.
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2. Proteins: Structure, Function, and Bioinformatics
3. Evolution of glutamate dehydrogenase genes: Evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life
4. A glutamate-dependent phenotype in E., coli K12: The result of two mutations
5. Characterization of Hydrogenase from the Hyperthermophilic Archaebacterium, Pyrococcus furiosus
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1. Glutamate dehydrogenase from hyperthermophilic Bacteria and Archaea: determinants of thermostability and catalysis at extremely high temperatures;Journal of Molecular Catalysis B: Enzymatic;1999-09
2. The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic ArchaeonPyrococcus furiosus Represents a Novel Site of Glycolytic Regulation;Journal of Biological Chemistry;1998-10
3. Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution;Journal of Molecular Biology;1997-04
4. Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli;Journal of Bacteriology;1995-12
5. Exchange of domains of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus and the mesophilic bacterium Clostridium difficile: effects on catalysis, thermoactivity and stability;"Protein Engineering, Design and Selection";1995
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