Modeling Enzyme Action—A Themed Honorary Issue to Prof. Fredric M. Menger
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Applied Chemistry".
Deadline for manuscript submissions: closed (15 August 2021) | Viewed by 19470
Special Issue Editor
2. Department of Sciences, University of Basilicata, Via dell’Ateneo Lucano 10, 85100 Potenza, Italy
Interests: design and synthesis of anticancer prodrugs with targeting properties determined by the linker’s type; design and synthesis of prodrugs with inefficient bioavailability; design and synthesis of prodrugs for masking the bitter sensation of commonly used drugs
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Special Issue Information
Dear Colleagues,
Molecules is pleased to announce a Special Issue dedicated to Fredric M. Menger, an emeritus professor of chemistry at Emory University, to celebrate his outstanding contribution to the synthesis and examination of organic systems and materials with biological importance. Among the projects that have emerged from his research group over the years are the following: (a) naming, synthesizing, and characterizing gemini surfactants; (b) quantitatively formulating the pseudo-phase model of micellar reactions; (c) reconstructing the conventional Hartley micelle model; (d) devising the 1,4-di-13C NMR method for determining hydrocarbon-chain conformation; (e) using microemulsion systems to destroy chemical warfare agents; (f) applying light microscopy to monitor morphological changes, e.g., budding and birthing, in giant-vesicle membranes; (g) correcting the classical Gibbs analysis of surface tension data; (h) constructing metallo-micelles and combinatorial metallo-polymers as enzyme models; (i) experimentally disproving the orbital steering theory of enzymes; (j) studying aqueous gels of small organic molecules via viscometric methods; (k) determining the kinetics of enzymes dissolved in heptane with water-pools; (l) evaluating the negative rate constant concept; (m) synthesizing delivery systems based on liposomes labile to specific enzymes; (n) introducing the role of distance in enzyme action; and (o) proposing an epigenetic model for the evolution of human intelligence.
The striking efficiency of enzyme catalysis has motivated several organic chemists to unravel enzyme mechanisms by exploring certain intra-molecular reactions, such as enzyme models that proceed faster than their corresponding intermolecular counterparts. This brings about the important question of whether enzyme models have the potential to replace natural enzymes. Today, the consensus is that the catalytic activity of an enzyme is based on the combined effects of catalysis by functional groups and the ability to reroute intermolecular reactions through alternative pathways by which substrates bind to preorganized active sites. Rate acceleration by enzymes can be due to (a) covalently enforced proximity, as in chymotrypsin, (b) non-covalently enforced proximity, as in the catalytic activity of metallo-enzymes, (c) covalently enforced strain, and (d) non-covalently enforced strain, which has been extensively studied in models that mimic the enzyme lysozyme.
The rate constants for a large majority of enzymatic reactions exceed their non-enzymatic bimolecular counterparts by 1010 to 1018 fold. For example, reactions catalyzed by cyclophilin are enhanced by 105 and those by orotidine monophosphatedecarboxylase are enhanced by 1017. The significant rate of acceleration achieved by enzymes is brought about by the binding of the substrate within the confines of the enzyme pocket called the active site. The binding energy of the resulting enzyme–substrate complex is the dominant driving force and the major contributor to catalysis. It is believed that in all enzymatic reactions, binding energy is used to overcome prominent physical and thermodynamic factors that create barriers for the reaction (ΔG). Both, enzymes and intra-molecular processes are similar in that the reacting centers are held together (covalently with intra molecular systems, and non-covalently with enzymes).
In this Special Issue “Modeling Enzyme Action—A Themed Honorary Issue to Prof. Fredric M. Menger”, the various strategies employed in modeling enzyme action will be reported. Both reviews and original research contributions will be accepted.
Prof. Dr. Rafik Karaman
Guest Editor
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Keywords
- enzyme models
- intramolecular processes
- enzymes mechanisms
- mimicking enzymes
