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Turnover number has two different meanings: In enzymology, turnover number (also termed ''k''cat) is defined as the maximum number of chemical conversions of substrate molecules per second that a single active site will execute for a given
enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products ...
concentration _T/math> for enzymes with two or more active sites. For enzymes with a single active site, ''k''cat is referred to as the catalytic constant. It can be calculated from the maximum reaction rate V_\max and catalyst site concentration _T/math> as follows: :k_\mathrm = \frac (See
Michaelis–Menten kinetics In biochemistry, Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named after German biochemist Leonor Michaelis and Canadian physician Maud Menten. The model takes the form of an equation describing the rat ...
). In other chemical fields, such as organometallic catalysis, turnover number (abbreviated ''TON'') has a different meaning: the number of moles of substrate that a mole of catalyst can convert before becoming inactivated. An ideal catalyst would have an infinite turnover number in this sense, because it would never be consumed. The term turnover frequency (abbreviated ''TOF'') is used to refer to the turnover per unit time, equivalent to the meaning of turnover number in enzymology. For most relevant industrial applications, the turnover frequency is in the range of 10−2 – 102 s−1 (103 – 107 s−1 for enzymes). The enzyme catalase has the largest turnover frequency, with values up to 4 × 107 s−1 having been reported. :TON = \frac :TOF = \frac


Turnover number of diffusion-limited enzymes

AChE is a
serine hydrolase Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. A defining characteristic of these enzymes is the presence of a particular serine at the active site, which ...
with a reported catalytic constant > 10,000/s. This implies that AChE reacts with acetylcholine at close to the diffusion-limited rate. Carbonic anhydrase is one of the fastest enzymes, and its rate is typically limited by the
diffusion Diffusion is the net movement of anything (for example, atoms, ions, molecules, energy) generally from a region of higher concentration to a region of lower concentration. Diffusion is driven by a gradient in Gibbs free energy or chemica ...
rate of its substrates. Typical catalytic constants for the different forms of this enzyme range between 104 and 106 reactions per second.


See also

* Catalysis


References

Enzyme kinetics Units of catalytic activity {{Science-stub