Enzymes are highly specific and usually catalyze only one type of reaction. An enzyme-catalyzed reaction is initiated when the enzyme binds to its substrate to form an enzyme-substrate complex. The catalytic property of an enzyme is based on its three-dimensional structure and on an active site...
Although each reaction catalyzed by these enzymes is initiated by this common step, their overall reactions (including racemization, beta-elimination of water, beta-elimination of ammonia, and cycloisomerization) as well as the stereochemical consequences (syn vs anti) of the beta-elimination reactions...
enzyme-catalyzed reactions. For each of these GO Terms, we extracted identifiers for the substrates involved in the reaction. If the GO Term definition stated that the reaction is reversible, we treated all reactants (including products) as substrates; if a reaction was labeled as irreversible,...
significantly lower than the concentration of the substrate (as when the number of taxis is far lower than the number of waiting passengers), the rate of an enzyme-catalyzed reaction is directly dependent on the enzyme concentration (part (b) of Figure 18.13 “Concentration versus Reaction Rate...
The reaction is zero order and is linearly dependent upon enzyme concentration. The charge transfer product complex of FACoA and acyl-CoA dehydrogenase is not stable and completely dissociates, as evidenced by the complete disappearance of the charge transfer electronic band with a first-order rate...
Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, ... changes of the enzyme active site and substrate strengthen the hydrogen bonds that stabilize the intermediate, thereby facilitating the proton transfer...
After screening the diverse library, optimization of weak substrates into potent substrates (step 2 in Fig. 1) can be performed before converting substrates into inhibitors because transition-state theory for enzyme-catalyzed reactions predicts that the inhibitory activity (Ki) of mechanism-based ...
Carbon nitride-catalyzed oxidative cleavage of carbon–carbon bond of α-hydroxy ketones with visible light and thermal radiation Haiying Zhan, Wenjie Liu, Minling Fu, Jinghe Cen, ... Hua Cao Pages 184-189 select article Understanding the molecular basics behind catalyst shaping: Preparation of sus...
The resulting changes in the reaction threshold cycle values (ΔCt) were compared to nonstressed control (dark blue bars). −log2 differences in Ct values (ΔΔCt) were plotted as fold changes. Significant changes (P < 0.01) are shown as blue (b) and yellow (c) bars for katE ...
The enzyme cleaves RNA at a specific phosphodiester bond with a catalytic rate that is >106-fold faster than the uncatalyzed reaction and achieves substrate saturation with Michaelis–Menten kinetics. Divalent metal ion, pH profiles, and mass spectrometric (MS) analysis indicate that the reaction ...