The Mechanism of Substrate and Coenzyme Binding to Clostridial Glutamate Dehydrogenase During Reductive Amination
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.603_b.x/fullpdf
Reference45 articles.
1. Studies of dissociation-association processes in clostridial glutamate dehydrogenase
2. The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation
3. Subunit assembly and active site location in the structure of glutamate dehydrogenase
4. The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination
5. Initial formation of a non-covalent enzyme-reagent complex during the inactivation of clostridial glutamate dehydrogenase by Ellman's reagent: determination of the enzyme's dissociation constant for the binary complex with NAD+ from protection studies
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