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A bioactive compound is a compound that has an effect on a living organism, tissue or cell, usually demonstrated by basic research in vitro or in vivo in the laboratory. While dietary nutrients are essential to life, bioactive compounds have not been proved to be essential – as the body can function without them – or because their actions are obscured by nutrients fulfilling the function.
Enzymes catalyze chemical reactions involving the substrate(s). In the case of a single substrate, the substrate bonds with the enzyme active site, and an enzyme-substrate complex is formed. The substrate is transformed into one or more products, which are then released from the active site. The active site is then free to accept another ...
In molecular biology, substrate presentation is a biological process that activates a protein. The protein is sequestered away from its substrate and then activated by release and exposure to its substrate. [1] [2] A substrate is typically the substance on which an enzyme acts but can also be a protein surface to which a ligand binds. In the ...
In biology, a substrate is the surface on which an organism (such as a plant, fungus, or animal) lives.A substrate can include biotic or abiotic materials and animals. For example, encrusting algae that lives on a rock (its substrate) can be itself a substrate for an animal that lives on top of the algae.
The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...
The nucleophilic lysine residue is commonly targeted site in protein bioconjugation, typically through amine-reactive N-hydroxysuccinimidyl (NHS) esters. [3] To obtain optimal number of deprotonated lysine residues, the pH of the aqueous solution must be below the pKa of the lysine ammonium group, which is around 10.5, so the typical pH of the reaction is about 8 and 9.
The substrate is activated in a small part of the enzyme's macromolecule called the active site. There, the binding of a substrate close to functional groups in the enzyme causes catalysis by so-called proximity effects. It is possible to create similar catalysts from small molecules by combining substrate-binding
Increasing the substrate concentration increases the rate of reaction (enzyme activity). However, enzyme saturation limits reaction rates. An enzyme is saturated when the active sites of all the molecules are occupied most of the time. At the saturation point, the reaction will not speed up, no matter how much additional substrate is added.