NDLI: Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.

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Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.

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Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bell, Ellis Marion, Jimmy Wacker, Sarah A. Bradley, Michael J.
Description	Country affiliation: United States Author Affiliation: Wacker SA ( Biochemistry and Molecular Biology Program, Department of Chemistry, University of Richmond, Richmond, Virginia 23173, USA.)
Abstract	Bovine glutamate dehydrogenase (GDH) is allosterically regulated and requires substrate-induced subunit interactions for maximum catalytic activity. Steady-state and presteady-state kinetics indicate that the rate-limiting step depends on the nature of the substrate and are likely associated with conformational fluctuations necessary for optimal hydride transfer. Deuterated glutamate shows a steady-state isotope effect but no effect on the presteady-state burst rate, demonstrating that conformational effects are rate limiting for hydride transfer while product release is overall rate limiting for glutamate. Guanidine hydrochloride unfolding, heat inactivation, and differential scanning calorimetry demonstrate the effects of alternative substrates, glutamate and norvaline, on conformational stability. Glutamate has little effect on overall stability, whereas norvaline markedly stabilizes the protein. Limited proteolysis demonstrates that glutamate had a variety of effects on local flexibility, whereas norvaline significantly decreased conformational fluctuations that allow protease cleavage. Dynamic light scattering suggests that norvaline stabilizes all interfaces in the hexamer, whereas glutamate had little effect on trimer-trimer interactions. The substrate glutamate exhibits negative cooperativity and complex allosteric regulation but has only minor effects on global GDH stability, while promoting certain local conformational fluctuations. In contrast, the substrate norvaline does not show negative cooperativity or allow allosteric regulation. Instead, norvaline significantly stabilizes the enzyme and markedly slows or prevents local conformational fluctuations that are likely to be important for cooperative effects and to determine the overall rate of hydride transfer. This suggests that homotropic allosteric regulation by the enzymatic substrate involves changes in both global stability and local flexibility of the protein.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.459
Journal	Protein Science
Issue Number	10
Volume Number	19
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2010-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glutamate Dehydrogenase Chemistry Metabolism Protein Conformation Allosteric Regulation Animals Biocatalysis Calorimetry, Differential Scanning Circular Dichroism Enzyme Activation Enzyme Stability Drug Effects Glutamic Acid Guanidine Pharmacology Hot Temperature Kinetics Ligands Models, Molecular Protein Binding Protein Folding Substrate Specificity Valine Analogs & Derivatives Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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