Thermodynamic interaction parameters of a reactive enzyme ternary complex: glutamate dehydrogenase-NADPH-α-ketoglutarate
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(80)80483-2/fullpdf
Reference10 articles.
1. Thermodynamics of dehydrogenase reactions
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1. Enzymatic reaction sequences as coupled multiple traces on a multidimensional landscape;Trends in Biochemical Sciences;2008-03
2. A Unifying Model of the Thermodynamics of Formation of Dehydrogenase-Ligand Complexes;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Detection of Multiple Active Site Domain Motions in Transient-State Component Time Courses of the Clostridium symbiosum l-Glutamate Dehydrogenase-Catalyzed Oxidative Deamination Reaction;Biochemistry;2002-08-22
4. Mechanism of formation of bound alpha-iminoglutarate from alpha-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition.;Journal of Biological Chemistry;1988-02
5. The anomalous properties of the glutamate dehydrogenase-NADPH-alpha-ketoglutarate complex are not ascribable to a carbonyl addition reaction.;Journal of Biological Chemistry;1987-08
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