Coenzyme



  Coenzymes are small haem groups. Both coenzymes and prosthetic groups are types of the broader group of cofactors, which are any non-protein molecules (usually organic molecules or metal ions) that are required by an enzyme for its activity.[2]

In kinases dephosphorylate the ATP and convert it back to ADP.

Coenzymes molecules are often RNA world.

Coenzymes as metabolic intermediates

  Metabolism involves a vast array of chemical reactions, but most fall under a few basic types of reactions that involve the transfer of functional groups.[3] This common chemistry allows cells to use a small set of metabolic intermediates to carry chemical groups between different reactions.[4] These group-transfer intermediates are the coenzymes.

Each class of group-transfer reaction is carried out by a particular coenzyme, which is the substrate for a set of enzymes that produce it, and a set of enzymes that consume it. An example of this are the dehydrogenases that use reduce NAD+ to NADH. This reduced coenzyme is then a substrate for any of the reductases in the cell that need to reduce their substrates.[5]

Coenzymes are therefore continuously recycled as part of metabolism. As an example, the total quantity of ATP in the human body is about 0.1 hydrolysis of 100 to 150 moles of ATP daily which is around 50 to 75 kg. Typically, a human will use up their body weight of ATP over the course of the day.[6] This means that each ATP molecule is recycled 1000 to 1500 times daily.

Types

Coenzymes are the major role in organisms of methanogens, which are restricted to this group of archaea.[8]

Vitamins and derivatives

Coenzyme Vitamin Additional component Chemical group(s) transferred Distribution
Electrons Bacteria, archaea and eukaryotes
acyl groups Bacteria, archaea and eukaryotes
Tetrahydrofolic acid [10] formyl, methylene and formimino groups Bacteria, archaea and eukaryotes
electrons Bacteria, archaea and eukaryotes
Electrons Bacteria, archaea and eukaryotes
Coenzyme F420 [13] Methanogens and some bacteria

Non-vitamins

Coenzyme Chemical group(s) transferred Distribution
Phosphate group Bacteria, archaea and eukaryotes
Methyl group Bacteria, archaea and eukaryotes
3'-Phosphoadenosine-5'-phosphosulfate [16] Sulfate group Bacteria, archaea and eukaryotes
Electrons Bacteria, archaea and eukaryotes
Tetrahydrobiopterin [18] electrons Bacteria, archaea and eukaryotes
Cytidine triphosphate [19] Diacylglycerols and lipid head groups Bacteria, archaea and eukaryotes
Nucleotide sugars [20] Monosaccharides Bacteria, archaea and eukaryotes
Electrons Some bacteria and most eukaryotes
Coenzyme M [23][24] Methanogens
Coenzyme B [25] Methanogens
Methanofuran [26] Methanogens
Tetrahydromethanopterin [27] Methanogens

Evolution

Further information: Abiogenesis

Coenzymes, such as last universal ancestor, which lived about 4 billion years ago.[29][30]

Coenzymes may have been present even earlier in the history of life on Earth.[31] Interestingly, the nucleotide domains, which had originally evolved to bind a different cofactor.[34] This process of adapting a pre-evolved structure for a novel use is referred to as exaptation.

History

Further information: History of biochemistry

The first coenzyme to be discovered was NAD+, which was identified by Arthur Harden and William Youndin 1906.[35] They noticed that adding boiled and filtered nucleotide sugar phosphate by Hans von Euler-Chelpin.[36] Other coenzymes were identified throughout the early 20th century, with ATP being isolated in 1929 by Karl Lohmann,[37] and coenzyme A being discovered in 1945 by Fritz Albert Lipmann.[38]

The functions of coenzymes were at first mysterious, but in 1936, Otto Heinrich Warburg identified the function of NAD+ in hydride transfer.[39] This discovery was followed in the early 1940s by the work of Herman Kalckar, who established the link between the oxidation of sugars and the generation of ATP.[40] This confirmed the central role of ATP in energy transfer that had been proposed by Fritz Albert Lipmann in 1941.[41] Later, in 1949, Morris Friedkin and Albert L. Lehninger proved that the coenzyme NAD+ linked metabolic pathways such as the citric acid cycle and the synthesis of ATP.[42]

See also

References

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  2. ^ de Bolster, M.W.G. (1997). Glossary of Terms Used in Bioinorganic Chemistry: Cofactors. International Union of Pure and Applied Chemistry. Retrieved on 2007-10-30.
  3. ^ Mitchell P (1979). "The Ninth Sir Hans Krebs Lecture. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems". Eur J Biochem 95 (1): 1-20. PMID 378655.
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  15. ^ Chiang P, Gordon R, Tal J, Zeng G, Doctor B, Pardhasaradhi K, McCann P (1996). "S-Adenosylmethionine and methylation". FASEB J 10 (4): 471-80. PMID 8647346.
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  25. ^ Noll KM, Rinehart KL, Tanner RS, Wolfe RS (1986). "Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum". Proc. Natl. Acad. Sci. U.S.A. 83 (12): 4238–42. PMID 3086878.
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This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Coenzyme". A list of authors is available in Wikipedia.