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2. Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus. Robb FT, Park JB, Adams MW. Biochim Biophys Acta; 1992 Apr 17; 1120(3):267-72. PubMed ID: 1576153 [Abstract] [Full Text] [Related]
3. Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Consalvi V, Chiaraluce R, Politi L, Vaccaro R, De Rosa M, Scandurra R. Eur J Biochem; 1991 Dec 18; 202(3):1189-96. PubMed ID: 1765079 [Abstract] [Full Text] [Related]
4. Purification and properties of an extreme thermostable glutamate dehydrogenase from the archaebacterium Sulfolobus solfataricus. Schinkinger MF, Redl B, Stöffler G. Biochim Biophys Acta; 1991 Jan 23; 1073(1):142-8. PubMed ID: 1899341 [Abstract] [Full Text] [Related]
5. Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents. Kujo C, Ohshima T. Appl Environ Microbiol; 1998 Jun 23; 64(6):2152-7. PubMed ID: 9603828 [Abstract] [Full Text] [Related]
6. Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic Archaeon, ES4. DiRuggiero J, Robb FT, Jagus R, Klump HH, Borges KM, Kessel M, Mai X, Adams MW. J Biol Chem; 1993 Aug 25; 268(24):17767-74. PubMed ID: 8349661 [Abstract] [Full Text] [Related]
18. Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Consalvi V, Chiaraluce R, Politi L, Gambacorta A, De Rosa M, Scandurra R. Eur J Biochem; 1991 Mar 14; 196(2):459-67. PubMed ID: 1901040 [Abstract] [Full Text] [Related]
19. Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis. Cacciapuoti G, Bertoldo C, Brio A, Zappia V, Porcelli M. Extremophiles; 2003 Apr 14; 7(2):159-68. PubMed ID: 12664268 [Abstract] [Full Text] [Related]
20. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V. Structure; 1995 Nov 15; 3(11):1147-58. PubMed ID: 8591026 [Abstract] [Full Text] [Related] Page: [Next] [New Search]