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Allosteric Regulation of Proteases
ChemBioChem, 2008AbstractAllostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small‐molecule activators or inhibitors of proteases and are therefore of wide ...
Michael Ehrmann, Markus Kaiser
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Ribonucleotide Reductases: The Evolution of Allosteric Regulation
Archives of Biochemistry and Biophysics, 2002Ribonucleotide reductases catalyze in all living organisms the production of the deoxyribonucleotides required for DNA replication and repair. Their appearance during evolution was a prerequisite for the transition from the "RNA world," where RNA sufficed for both catalysis and information transfer, to today's situation where life depends on the ...
Peter Reichard
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Engineering Allosteric Regulation into Biological Catalysts
ChemBioChem, 2009AbstractEnzymes and ribozymes constitute two classes of biological catalysts. The activity of many natural enzymes is regulated by the binding of ligands that have different structures than their substrates; these ligands are consequently called allosteric effectors.
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Allosteric regulation of chaperonins
Current Opinion in Structural Biology, 2005Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling ...
Horovitz, A, Willison, KR
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Aptamers for allosteric regulation
Nature Chemical Biology, 2011Aptamers are useful for allosteric regulation because they are nucleic acid-based structures in which ligand binding induces conformational changes that may alter the function of a connected oligonucleotide at a distant site. Through this approach, a specific input is efficiently converted into an altered output.
Vinkenborg, J. +2 more
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Diversity of Allosteric Regulation in Proteases
ACS Chemical Biology, 2012Allostery is a fundamental regulatory mechanism that is based on a functional modulation of a site by a distant site. Allosteric regulation can be triggered by binding of diverse allosteric effectors, ranging from small molecules to macromolecules, and is therefore offering promising opportunities for functional modulation in a wide range of ...
Merdanovic, Melisa +3 more
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Engineered Allosteric Regulation of Protein Function
Journal of Molecular Biology, 2022Allosteric regulation of proteins has been utilized to study various aspects of cell signaling, from unicellular events to organism-wide phenotypes. However, traditional methods of allosteric regulation, such as constitutively active mutants and inhibitors, lack tight spatiotemporal control.
Jordan, Fauser +3 more
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The role of dynamics in allosteric regulation
Current Opinion in Structural Biology, 2003The biomolecular conformational changes often associated with allostery are, by definition, dynamic processes. Recent publications have disclosed the role of pre-existing equilibria of conformational substates in this process. In addition, the role of dynamics as an entropic carrier of free energy of allostery has been investigated.
Dorothee, Kern, Erik R P, Zuiderweg
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NADPH Is an Allosteric Regulator of HSCARG
Journal of Molecular Biology, 2009NADP(H) is an important cofactor that controls many fundamental cellular processes. We have determined the crystal structure of HSCARG, a novel NADPH sensor, and found that it forms an asymmetrical dimer with only one subunit occupied by an NADPH molecule, and the two subunits have dramatically different conformations.
Xueyu, Dai +8 more
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Allosteric regulation of phosphoribulokinase activity
Biochemical and Biophysical Research Communications, 1968Inhibition of ATP-dependent CO2 fixation by AMP has been reported in several autotrophic organisms (Johnson and Peck, 1965; Mayeux and Johnson, 1966;Johnson, 1966; Gale and Beck, 1966). Johnson (1966) suggested that the site of AMP inhibition is phosphoribulokinase and that inhibition may occur through allosteric modification of the enzyme. In contrast,
R D, MacElroy +2 more
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