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Journal Abstract Search

168 related items for PubMed ID: 1764463

  • 1. Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum.
    Syed SE, Engel PC, Parker DM.
    Biochim Biophys Acta; 1991 Dec 06; 1115(2):123-30. PubMed ID: 1764463
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  • 2. Kinetic studies on the binding of 1,N6-etheno-NAD+ to glutamate dehydrogenase from Clostridium symbiosum.
    Basso LA, Engel PC, Walmsley AR.
    Biochim Biophys Acta; 1997 Jun 20; 1340(1):63-71. PubMed ID: 9217015
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  • 3. Kinetic studies of dogfish liver glutamate dehydrogenase.
    Electricwala AH, Dickinson FM.
    Biochem J; 1979 Feb 01; 177(2):449-59. PubMed ID: 35153
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  • 4. Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate.
    Engel PC, Dalziel K.
    Biochem J; 1970 Jul 01; 118(3):409-19. PubMed ID: 4394334
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  • 5. The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during reductive amination.
    Basso LA, Engel PC, Walmsley AR.
    Eur J Biochem; 1995 Dec 01; 234(2):603-15. PubMed ID: 8536710
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  • 12. Intersubunit communication in hybrid hexamers of K89L/A163G/S380A and C320S mutants of glutamate dehydrogenase from Clostridium symbiosum.
    Goyal A, Aghajanian S, Hayden BM, Wang XG, Engel PC.
    Biochemistry; 1997 Dec 02; 36(48):15000-5. PubMed ID: 9398225
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  • 14. Re-engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzyme.
    Capone M, Scanlon D, Griffin J, Engel PC.
    FEBS J; 2011 Jul 02; 278(14):2460-8. PubMed ID: 21564547
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  • 15. The changed pattern of substrate specificity in the K89L mutant of glutamate dehydrogenase of Clostridium symbiosum.
    Wang XG, Dean JL, Engel PC, Baker PJ, Britton KL, Stillman TJ, Rice DW.
    Biochem Soc Trans; 1994 Aug 02; 22(3):320S. PubMed ID: 7821579
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  • 16. The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination.
    Basso LA, Engel PC, Walmsley AR.
    Eur J Biochem; 1993 May 01; 213(3):935-45. PubMed ID: 8099328
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  • 17. Positive cooperativity with Hill coefficients of up to 6 in the glutamate concentration dependence of steady-state reaction rates measured with clostridial glutamate dehydrogenase and the mutant A163G at high pH.
    Wang XG, Engel PC.
    Biochemistry; 1995 Sep 12; 34(36):11417-22. PubMed ID: 7547869
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  • 18. Steady-state kinetics and transient studies of substrate and coenzyme analogue binding to clostridial glutamate dehydrogenase (GDH) during oxidative deamination.
    Basso LA, Engel PC, Walmsley AR.
    Biochem Soc Trans; 1994 Aug 12; 22(3):319S. PubMed ID: 7821578
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  • 19. Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding.
    Syed SE, Hornby DP, Brown PE, Fitton JE, Engel PC.
    Biochem J; 1994 Feb 15; 298 ( Pt 1)(Pt 1):107-13. PubMed ID: 8129708
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