Results 261 to 270 of about 57,293 (304)

Dihydroorotase from Clostridiumoroticum is an allosteric enzyme

Biochemical and Biophysical Research Communications, 1979
Abstract Dihydroorotase from Clostridium oroticum exhibits allosteric behavior with respect to both of its substrates. L-dihydroorotate dependence reflects a positive homotropic interaction for which the Hill coefficient is 1.3–1.6, depending upon the preparation.
J E, Scheffler, J, Ma, E G, Sander
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Yeast chorismate and other allosteric enzymes

Pure and Applied Chemistry, 1998
Abstract
William N. Lipscomb, Norbert Sträter
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Allosteric properties of enzymes with “ping-pong” mechanism

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract Allosteric properties of enzymes exhibiting the ping-pong mechanism, which is characterized by the oscillation of enzyme protein between multiple stable enzyme forms during reaction, have been analyzed in terms of the partial equilibrium theory recently introduced by Cha ( J. Biol. Chem. , 243 (1968) 820).
T, Sumi, M, Ui
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The Kinetics of Allosteric Enzymes

1977
Many important enzymes are oligomeric in structure, being more or less stable associations of smaller units, called protomers, each of which may have one or more than one active site. By comparing these enzymes with monomeric enzymes that have branched mechanisms, it can be seen intuitively that the possibility of binding substrate at more than one ...
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Kinetic Analysis of Allosteric Enzymes

1971
Publisher Summary Allosteric enzymes are defined as those enzymes that can mediate indirect interactions between distinct sites. They are characterized by a sigmoidal response of the initial rate to increasing substrate or inhibitor concentration. An increasing number of allosteric enzymes exhibit another type of deviation of the binding curves for ...
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Allosteric Enzyme- and Transporter-Based Interactions

2009
Allosterism in enzymes and transporters can result in alterations in kinetic profiles and in rates of metabolism and transport. Cooperativity due to allosteric interactions has been observed with drug-metabolizing enzymes such as the cytochromes P450 and the uridine glucuronosyltransferases.
Murali Subramanian, Timothy S. Tracy
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Metal–Organic Framework-Based Enzyme Biocomposites

Chemical Reviews, 2021
, Peter Wied, Francesco Carraro
exaly  

Bioinspired Framework Catalysts: From Enzyme Immobilization to Biomimetic Catalysis

Chemical Reviews, 2023
Kun-Yu Wang, Jiandong Pang, Wei Shi
exaly  

Expanding the Synthetic Toolbox through Metal–Enzyme Cascade Reactions

Chemical Reviews, 2023
Ivan Lavandera, Vicente Gotor-Fernández
exaly  

Visualizing allosteric pathways in oligomeric enzymes

2023
Visualizing molecular structures and their interactions is essential for understanding their function. A number of computer programs that serve this purpose have become indispensable tools in this niche. Programs such as Pymol, Chimera, and Coot, to mention perhaps the most known examples, all have their devoted followers based on their strengths and ...
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