Cooperativity in monomeric enzymes with single ligand-binding sites.
Carol M. Porter,Brian G. Miller +1 more
TLDR
The primary mechanisms postulated to give rise to monomeric cooperativity are discussed and modern experimental methods that could offer new insights into the nature of this phenomenon are highlighted.About:
This article is published in Bioorganic Chemistry.The article was published on 2012-08-01 and is currently open access. It has received 88 citations till now. The article focuses on the topics: Cooperativity.read more
Citations
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The Central Role of Glucokinase in Glucose Homeostasis: A Perspective 50 Years After Demonstrating the Presence of the Enzyme in Islets of Langerhans.
TL;DR: Having a common glucose sensor couples complementary regulatory mechanisms into a tightly regulated and stable glucose homeostatic network.
Journal ArticleDOI
Solution NMR Spectroscopy for the Study of Enzyme Allostery
George P. Lisi,J. Patrick Loria +1 more
TL;DR: NMR spectroscopy is unequaled in its ability to detect structural and dynamical changes in biomolecules, and the case studies presented herein demonstrate the range of insights to be gained from this valuable method.
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Changing the selectivity of p300 by acetyl-CoA modulation of histone acetylation.
TL;DR: This study investigates how changing acetyl-CoA concentrations alter the histone acetylation pattern by altering p300 specificity, and demonstrates how the p300 inhibitor C646 can pharmacologically alter p300 histoneacetylation patterns in vitro and in cells.
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Dual allosteric activation mechanisms in monomeric human glucokinase
A. Carl Whittington,Mioara Larion,Joseph M. Bowler,Kristen M. Ramsey,Rafael Brüschweiler,Brian G. Miller +5 more
TL;DR: This work elucidates specific structural features responsible for generating allostery in a monomeric enzyme and suggests a general strategy for engineering cooperativity into proteins that lack the structural framework typical of traditional allosteric systems.
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The Activating Oxydianion Binding Domain for Enzyme-Catalyzed Proton Transfer, Hydride Transfer, and Decarboxylation: Specificity and Enzyme Architecture
Archie C. Reyes,Xiang Zhai,Kelsey T. Morgan,Christopher J. Reinhardt,Tina L. Amyes,John P. Richard +5 more
TL;DR: The observation of dianion activation by stabilization of active caged Michaelis complexes may be generalized to the many other enzymes that utilize substrate binding energy to drive changes in enzyme conformation, which induce tight substrate fits.
References
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Dynamic personalities of proteins.
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Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy.
TL;DR: Dynamic structural changes of macromolecules undergoing biochemical reactions can be studied using novel single molecule spectroscopy tools using distance and orientation molecular rulers.
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Nonsense mutation in the glucokinase gene causes early-onset non-insulin-dependent diabetes mellitus
Nathalie Vionnet,Markus Stoffel,J. Takeda,K. Yasuda,Graeme I. Bell,Habib Zouali,Suzanne Lesage,Gilberto Velho,F. Iris,Ph. Passa,Philippe Froguel,David M. Cohen +11 more
TL;DR: The identification of a nonsense mutation in the gene encoding glucokinase and its linkage with early-onset diabetes in one family is reported, the first evidence implicating a mutation in a gene involved in glucose metabolism in the pathogenesis of NIDDM.
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Prolyl cis-trans isomerization as a molecular timer
TL;DR: Recent studies indicate that both phosphorylation-dependent and phosphorylated-independent prolyl cis-trans isomerization can act as a novel molecular timer to help control the amplitude and duration of a cellular process, and prolyL cis- trans isomerized proteins might be a new target for therapeutic interventions.