Redesigning allosteric activation in an enzyme [PDF]
Proceedings of the National Academy of Sciences, 2011 Enzyme activation by monovalent cations is widely documented in plants and the animal world. In type II enzymes, activation entails two steps: binding of the monovalent cation to its allosteric site and transduction of this event into enhanced catalytic activity.
Sadhna Rana +3 more
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Comparison of Plant-Type Phospho enol pyruvate Carboxylases from Rice: Identification of Two Plant-Specific Regulatory Regions of the Allosteric Enzyme [PDF]
Plant and Cell Physiology, 2014 Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme of primary metabolism in bacteria, algae and vascular plants, and it undergoes allosteric regulation by various metabolic effectors.
Masayuki Muramatsu +3 more
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Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation [PDF]
Journal of Biological Chemistry, 2009 The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast ...
S. Kutter +5 more
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A Novel Fold Revealed by Mycobacterium tuberculosis NAD Kinase, a Key Allosteric Enzyme in NADP Biosynthesis [PDF]
Journal of Biological Chemistry, 2004 NAD kinase catalyzes the magnesium-dependent phosphorylation of NAD, representing the sole source of freshly synthesized NADP in all organisms. The enzyme is essential for the growth of the deadly multidrug-resistant pathogen Mycobacterium tuberculosis ...
Silvia Garavaglia +4 more
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Substrate-Based Allosteric Regulation of a Homodimeric Enzyme
Journal of the American Chemical Society, 2019 Many enzymes operate through half-of-the sites reactivity wherein a single protomer is catalytically engaged at one time. In the case of the homodimeric enzyme, fluoroacetate dehalogenase, substrate binding triggers closing of a regulatory cap domain in the empty protomer, preventing substrate access to the remaining active site.
Pedram Mehrabi +11 more
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Journal of Enzyme Inhibition and Medicinal Chemistry, 2023 The formal mechanism of linear mixed and non-competitive enzyme inhibition implies the binding of inhibitors to both the active site of the free enzyme in competition with the substrate, and to an allosteric site on the enzyme-substrate complex. However,
Alessandro Pesaresi
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Dissecting the Allosteric Fine-Tuning of Enzyme Catalysis
JACS AuFully understanding the mechanism of allosteric regulation in biomolecules requires separating and examining all of the involved factors. In enzyme catalysis, allosteric effector binding shifts the structure and dynamics of the active site, leading to modified energetic (e.g., energy barrier) and dynamical (e.g., diffusion coefficient) factors ...
Xin-Qiu Yao, Donald Hamelberg
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Coevolution-based prediction of key allosteric residues for protein function regulation
eLife, 2023 Allostery is fundamental to many biological processes. Due to the distant regulation nature, how allosteric mutations, modifications, and effector binding impact protein function is difficult to forecast.
Juan Xie +4 more
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Fumarate analogs act as allosteric inhibitors of the human mitochondrial NAD(P)+-dependent malic enzyme. [PDF]
PLoS ONE, 2014 Human mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by the four-carbon trans dicarboxylic acid, fumarate. Previous studies have suggested that the dicarboxylic acid in a trans conformation around the carbon-carbon
Ju-Yi Hsieh +5 more
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The Cyclic Dinucleotide c-di-AMP Is an Allosteric Regulator of Metabolic Enzyme Function
Cell, 2014 Kamakshi Sureka +12 more
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