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In chemistry, a reaction coordinate [1] is an abstract one-dimensional coordinate chosen to represent progress along a reaction pathway. Where possible it is usually a geometric parameter that changes during the conversion of one or more molecular entities, such as bond length or bond angle. For example, in the homolytic dissociation of ...
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. 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.
Using an external PC has some downsides. For example, external PCs typically complicate reaction design because the PC may react with both the bound and unbound substrate. If a reaction occurs between the unbound substrate and the PC, enantioselectivity is lost and other side reactions may occur.
A catalytic triad is a set of three coordinated amino acid residues that can be found in the active site of some enzymes. [1] [2] Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases).
Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.
An example of heterogeneous catalysis is the reaction of oxygen and hydrogen on the surface of titanium dioxide (TiO 2, or titania) to produce water. Scanning tunneling microscopy showed that the molecules undergo adsorption and dissociation. The dissociated, surface-bound O and H atoms diffuse together.
For example, the most widely studied bacterium, E. coli strain K-12, is able to produce about 2,338 metabolic enzymes. [1] These enzymes collectively form a complex web of reactions comprising pathways by which substrates (including nutients and intermediates) are converted to products (other intermediates and end-products).
An example of an enzyme that contains a cofactor is carbonic anhydrase, which uses a zinc cofactor bound as part of its active site. [60] These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. [1]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions. [1]: 17