Turnover number

In enzymology, turnover number (also termed kcat) 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 concentration for enzymes with two or more active sites.[1] For enzymes with a single active site, kcat is referred to as the catalytic constant.[2] It can be calculated from the maximum reaction rate and catalyst site concentration as follows:

(See Michaelis-Menten kinetics).

Turnover number has two different meanings:

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.[3] An ideal catalyst would have an infinite turnover number in this sense, because it wouldn't ever be consumed, but in actual practice one often sees turnover numbers which go from 100 up to 40 million for catalase. The term turnover frequency (abbreviated TOF) is used to refer to the turnover per unit time, as in enzymology. For most relevant industrial applications, the turnover frequency is in the range of 10−2 – 102 s−1 (enzymes 103 – 107 s−1).[1] Turnover frequency of catalase is maximum i.e. 4 X 107 s−1.

Turnover number of diffusion-limited enzymes
See also: Diffusion limited enzyme

AChE is a serine hydrolase with a reported catalytic constant > 10,000/s. This implies that AChE reacts with acetylcholine at close to the diffusion-limited rate.[4]

Carbonic anhydrase is one of the fastest enzymes, and its rate is typically limited by the diffusion rate of its substrates. Typical catalytic constants for the different forms of this enzyme range between 104 and 106 reactions per second.[5]

See also

References
  1. Roskoski, Robert (2015-01-01), "Michaelis-Menten Kinetics☆", Reference Module in Biomedical Sciences, Elsevier, doi:10.1016/b978-0-12-801238-3.05143-6, ISBN 978-0-12-801238-3, retrieved 2020-12-15
  2. Leskovac V (2003). Comprehensive Enzyme Kinetics. New York, USA: Kluwer Academic/Plenum.
  3. Bligaard, Thomas; Bullock, R. Morris; Campbell, Charles T.; Chen, Jingguang G.; Gates, Bruce C.; Gorte, Raymond J.; Jones, Christopher W.; Jones, William D.; Kitchin, John R.; Scott, Susannah L. (2016). "Toward Benchmarking in Catalysis Science: Best Practices, Challenges, and Opportunities". ACS Catalysis. 6 (4): 2590–2602. doi:10.1021/acscatal.6b00183.
  4. Quinn DM (1987). "Acetylcholinesterase: Enzyme Structure, Reaction Dynamics, and Virtual Transition States". Chemical Reviews. 87: 955–79. doi:10.1021/bi00349a019.
  5. Lindskog S (1997). "Structure and mechanism of carbonic anhydrase". Pharmacology & Therapeutics. 74 (1): 1–20. doi:10.1016/S0163-7258(96)00198-2. PMID 9336012.


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