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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 ...
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).
Catalysis (/ k ə ˈ t æ l ə s ɪ s /) is the increase in rate of a chemical reaction due to an added substance known as a catalyst [1] [2] (/ ˈ k æ t əl ɪ s t /). Catalysts are not consumed by the reaction and remain unchanged after it. [ 3 ]
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.
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.
The catalytic cycle is the main method for describing the role of catalysts in biochemistry, organometallic chemistry, bioinorganic chemistry, materials science, etc. Since catalysts are regenerated, catalytic cycles are usually written as a sequence of chemical reactions in the form of a loop.
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