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Journal Abstract Search

146 related items for PubMed ID: 8099328

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2. 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
    [Abstract] [Full Text] [Related]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. 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 20; 22(3):319S. PubMed ID: 7821578
    [No Abstract] [Full Text] [Related]

  • 5. A difference in the sequence of steps in the reactions catalyzed by two closely homologous forms of glutamate dehydrogenase.
    Maniscalco SJ, Saha SK, Vicedomine P, Fisher HF.
    Biochemistry; 1996 Jan 09; 35(1):89-94. PubMed ID: 8555203
    [Abstract] [Full Text] [Related]

  • 6. Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes.
    Bell ET, LiMuti C, Renz CL, Bell JE.
    Biochem J; 1985 Jan 01; 225(1):209-17. PubMed ID: 2858197
    [Abstract] [Full Text] [Related]

  • 7. A kinetic study of the oxidative deamination of L-glutamate by Peptostreptococcus asaccharolyticus glutamate dehydrogenase using a variety of coenzymes.
    Hornby DP, Engel PC.
    Eur J Biochem; 1984 Sep 17; 143(3):557-60. PubMed ID: 6148240
    [Abstract] [Full Text] [Related]

  • 8. The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.
    Hornby DP, Aitchison MJ, Engel PC.
    Biochem J; 1984 Oct 01; 223(1):161-8. PubMed ID: 6149744
    [Abstract] [Full Text] [Related]

  • 9. Importance of glutamate 279 for the coenzyme binding of human glutamate dehydrogenase.
    Yoon HY, Cho EH, Kwon HY, Choi SY, Cho SW.
    J Biol Chem; 2002 Nov 01; 277(44):41448-54. PubMed ID: 12193607
    [Abstract] [Full Text] [Related]

  • 10. Detection of multiple active site domain motions in transient-state component time courses of the Clostridium symbiosum L-glutamate dehydrogenase-catalyzed oxidative deamination reaction.
    Tally JF, Maniscalco SJ, Saha SK, Fisher HF.
    Biochemistry; 2002 Sep 17; 41(37):11284-93. PubMed ID: 12220195
    [Abstract] [Full Text] [Related]

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  • 15. The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.
    Lilley KS, Engel PC.
    Eur J Biochem; 1992 Jul 15; 207(2):533-40. PubMed ID: 1633808
    [Abstract] [Full Text] [Related]

  • 16. 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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  • 17. 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 01; 22(3):320S. PubMed ID: 7821579
    [No Abstract] [Full Text] [Related]

  • 18. Reaction mechanism of L-glutamate dehydrogenase. Transient complexes in the oxidative deamination of L-glutamate catalyzed by NAD(P)-dependent L-glutamate dehydrogenase.
    Di Franco A.
    Eur J Biochem; 1974 Jun 15; 45(2):407-24. PubMed ID: 4153036
    [No Abstract] [Full Text] [Related]

  • 19. Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction.
    Andersson P, Kvassman J, Oldén B, Pettersson G.
    Eur J Biochem; 1984 Mar 15; 139(3):519-27. PubMed ID: 6365555
    [Abstract] [Full Text] [Related]

  • 20. Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis.
    Nidetzky B, Klimacek M, Mayr P.
    Biochemistry; 2001 Aug 28; 40(34):10371-81. PubMed ID: 11513616
    [Abstract] [Full Text] [Related]

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