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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. Most enzymes are proteins, and most such processes are chemical reactions.
Most enzymes have a rate around 10 5 s −1 M −1. The fastest enzymes in the dark box on the right (>10 8 s −1 M −1) are constrained by the diffusion limit. (Data adapted from reference [1]) A diffusion-limited enzyme catalyses a reaction so efficiently that the rate limiting step is that of substrate diffusion into the active site, or ...
Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.
NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD +).Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase.
In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]
This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:carnitine O-acetyltransferase. Other names in common use include acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine transferase, carnitine acetyl ...
In enzymology, a (carboxyethyl)arginine β-lactam-synthase (EC 6.3.3.4) is an enzyme that catalyzes the chemical reaction ATP + L - N 2 -(2-carboxyethyl)arginine ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + deoxyamidinoproclavaminate
Although general-acid catalysis for breakdown of the First and Second tetrahedral intermediate may occur by the path shown in the diagram, evidence supporting such a mechanism with chymotrypsin [25] has been controverted. [26] The second stage of catalysis is the resolution of the acyl-enzyme intermediate by the attack of a second substrate.