Molecular basis of enzyme action and inhibition
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Molecular basis of enzyme action and inhibition

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Published by Macmillan in New York .
Written in English


  • Enzymes -- Congresses.,
  • Enzyme inhibitors -- Congresses.

Book details:

Edition Notes

Statementedited by P.A.E. Desnuelle.
SeriesI.U.B. symposium series -- v. 24., Its Proceedings -- v. 4.
ContributionsDesnuelle, P.
The Physical Object
Paginationxvi, 343 p. :
Number of Pages343
ID Numbers
Open LibraryOL16988860M

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The pharmacological action of drugs is mainly based on enzyme inhibition, e.g. sulfonamides and other antibiotics. In the majority of cases the enzyme inhibited is known. The development of nerve gases, insecticides and herbicides is based on enzyme inhibition studies. Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents. Khan JA(1), Tao X, Tong L. Author information: (1)Department of Biological Sciences, Columbia University, New York, New York , USA. Comment in Nat Struct Mol Biol. Jul;13(7)Cited by: 1) CO 2 + H 2 O ← Carbonic anhydrase H 2 CO 3 {\displaystyle {\ce {CO2{}+H2O. Terms from the book Biochemistry: The Molecular Basis of Life 5th Ed. Terms in this set (42) activation energy. the threshold energy required to produce a chemical reaction. a form of enzyme inhibition in which the inhibitory effect of a compound can be counteracted by increasing substrate or removing the inhibitor while the enzyme remains.

Chemical and Molecular Basis of Nerve Activity contains 16 chapters that discuss the significant advances in the study of the molecular events underlying bioelectricity and nerve excitability. After briefly describing the physiology and mechanisms of the nervous system, this book goes on examining the physiologically significant features and. Absolute specificity - the enzyme will catalyze only one reaction. 2. Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino, phosphate and methyl groups. 3. Linkage specificity - the enzyme will act on a particular type of chemical bond regardless of the rest of the molecular structure. Size: KB. THE MOLECULAR BASIS FOR ENZYME REGULATION TABLE I1 (Continued) Diagnostic test, Activator Observation Conclusion ~ ~- J which is not a substrate in- J probably induces conformacreases velocity or affinity tional change-in special of X I cases, e.g., metal ion, may take direct part in catalytic action Competitive May compete directly a t act Cited by: In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time, as shown in the figure on the usually results from the inhibitor having an affinity for the active site of an enzyme where the substrate also binds; the substrate and inhibitor compete for access to the enzyme's active site. This type of inhibition can be overcome by sufficiently high.

The activity of many enzymes can be inhibited by the binding of specific small molecules and ions. This means of inhibiting enzyme activity serves as a major control mechanism in biological systems. The regulation of allosteric enzymes typifies this type of control. In addition, many drugs and toxic agents act by inhibiting enzymes. Inhibition by particular chemicals can be a source Cited by: 6. Docking is a powerful approach to perform virtual screening on large library of compounds, rank the conformations using a scoring function, and propose structural hypotheses of how the ligands inhibit the target, which is invaluable in lead optimization. Using experimentally proven active compounds, detailed docking studies were performed to determine the mechanism of Cited by: 1. 4 Enzyme Inhibition and Bioapplications enzyme inhibition action and physiological regulation of metabolic enzymes as evidenced in following chapters in this book. Some notable classic examples are: drug and toxin action and/or drug design for therapeutic uses e.g., iodoacetamide deactiva tes cys amino acid in. In reversible inhibition, for example, in the action of malonic acid on succinic dehydrogenase, the enzyme’s activity is restored when the inhibitor is eliminated by dialysis or by another method. In irreversible inhibition the action of the inhibitor, even when the inhibitor is present in very low concentrations, is gradually intensified and.