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11-SEPTEMBER-2008 13:54:10 - Coenzyme Coenzyme A Coenzyme A Coenzymes are small organic non-protein molecules that carry chemical groups between enzymes.1 Coenzymes are sometimes referred to as cosubstrates. These molecules are substrates for enzymes and do not form a permanent part of the enzymes' structures. This distinguishes coenzymes from prosthetic groups, which are non-protein components that are bound tightly to enzymes - such as iron-sulfur centers, flavin or 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 metabolism, coenzymes are involved in both group-transfer reactions, for example coenzyme A and adenosine triphosphate ATP, and redox reactions, such as coenzyme Q10 and nicotinamide adenine dinucleotide NAD+. Coenzymes are consumed and recycled continuously in metabolism, with one set of enzymes adding a chemical group to the coenzyme and another set removing it. For example, enzymes such as ATP synthase continuously phosphorylate adenosine diphosphate ADP, converting it into ATP, while enzymes such as kinases dephosphorylate the ATP and convert it back to ADP. Coenzymes molecules are often vitamins or are made from vitamins. Many coenzymes contain the nucleotide adenosine as part of their structures, such as ATP, coenzyme A and NAD+. This common structure may reflect a common evolutionary origin as part of ribozymes in an ancient RNA world. Contents 1 Coenzymes as metabolic intermediates 2 Types 2.1 Vitamins and derivatives 2.2 Non-vitamins 3 Evolution 4 History 5 See also 6 References 7 External links Coenzymes as metabolic intermediates The redox reactions of nicotinamide adenine dinucleotide. The redox reactions of nicotinamide adenine dinucleotide. 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 nicotinamide adenine dinucleotide NADH as a cofactor. Here, hundreds of separate types of enzymes remove electrons from their substrates and 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 mole. This ATP is constantly being broken down into ADP, and then converted back into ATP. Thus, at any given time, the total amount of ATP + ADP remains fairly constant. The energy used by human cells requires the 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 Acting as coenzymes in organisms is the major role of vitamins, although vitamins do have other functions in the body.7 Coenzymes are also commonly made from nucleotides: such as adenosine triphosphate, the biochemical carrier of phosphate groups, or coenzyme A, the coenzyme that carries acyl groups. Most coenzymes are found in a huge variety of species, and some are universal to all forms of life. An exception to this wide distribution is a group of unique coenzymes that evolved in methanogens, which are restricted to this group of archaea.8 Vitamins and derivatives Coenzyme Vitamin Additional component Chemical groups transferred Distribution NAD+ and NADP+ 5 Niacin B3 ADP Electrons Bacteria, archaea and eukaryotes Coenzyme A 9 Pantothenic acid B5 ADP Acetyl group and other acyl groups Bacteria, archaea and eukaryotes Tetrahydrofolic acid 10 Folic acid B9 Glutamate residues Methyl, formyl, methylene and formimino groups Bacteria, archaea and eukaryotes Menaquinone 11 Vitamin K None Carbonyl group and electrons Bacteria, archaea and eukaryotes Ascorbic acid 12 Vitamin C None Electrons Bacteria, archaea and eukaryotes Coenzyme F420 13 Riboflavin B2 Amino acids Electrons Methanogens and some bacteria Non-vitamins Coenzyme Chemical groups transferred Distribution Adenosine triphosphate 14 Phosphate group Bacteria, archaea and eukaryotes S-Adenosyl methionine 15 Methyl group Bacteria, archaea and eukaryotes 3'-Phosphoadenosine-5'-phosphosulfate 16 Sulfate group Bacteria, archaea and eukaryotes Coenzyme Q 17 Electrons Bacteria, archaea and eukaryotes Tetrahydrobiopterin 18 Oxygen atom and 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 Glutathione 2122 Electrons Some bacteria and most eukaryotes Coenzyme M 2324 Methyl group Methanogens Coenzyme B 25 Electrons Methanogens Methanofuran 26 Formyl group Methanogens Tetrahydromethanopterin 27 Methyl group Methanogens Evolution Further information: Abiogenesis Coenzymes, such as ATP and NADH, are present in all known forms of life and form a core part of metabolism. Such universal conservation indicates that these molecules evolved very early in the development of living things.28 At least some of the current set of coenzymes may therefore have been present in the last universal ancestor, which lived about 4 billion years ago.2930 Coenzymes may have been present even earlier in the history of life on Earth.31 Interestingly, the nucleotide adenosine is present in coenzymes that catalyse many basic metabolic reactions such as methyl, acyl, and phosphoryl group transfer, as well as redox reactions. This ubiquitous chemical scaffold has therefore been proposed to be a remnant of the RNA world, with early ribozymes evolving to bind a restricted set of nucleotides and related compounds.3233 Adenosine-based coenzymes are thought to have acted as interchangeable adaptors that allowed enzymes and ribozymes to bind new coenzymes through small modifications in existing adenosine-binding 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 yeast extract greatly accelerated alcoholic fermentation in unboiled yeast extracts. They called the unidentified factor responsible for this effect a coferment. Through a long and difficult purification from yeast extracts, this heat-stable factor was identified as a 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 Cofactor Enzymes Adenosine triphosphate References ^ de Bolster, M.W.G. 1997. Glossary of Terms Used in Bioinorganic Chemistry: Coenzymes. International Union of Pure and Applied Chemistry. Retrieved on 2007-10-30. ^ 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. ^ 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. doi:10.1111/j.1432-1033.1979.tb12934.x. PMID 378655. ^ Wimmer M, Rose I. Mechanisms of enzyme-catalyzed group transfer reactions. Annu Rev Biochem 47: 1031-78. doi:10.1146/annurev.bi.47.070178.005123. PMID 354490. ^ a b Pollak N, Dölle C, Ziegler M 2007. The power to reduce: pyridine nucleotides--small molecules with a multitude of functions. Biochem. J. 402 2: 205-18. doi:10.1042/BJ20061638. PMID 17295611. ^ Di Carlo, S. E. and Coliins, H. L. 2001 Estimating ATP resynthesis during a marathon run: a method to introduce metabolism Advan. Physiol. Edu. 25: 70-71. ^ Bolander FF 2006. Vitamins: not just for enzymes. Curr Opin Investig Drugs 7 10: 912-5. PMID 17086936. ^ Rouvière PE, Wolfe RS 1988. Novel biochemistry of methanogenesis. J. Biol. Chem. 263 17: 7913-6. PMID 3131330. ^ Leonardi R, Zhang YM, Rock CO, Jackowski S 2005. Coenzyme A: back in action. Prog. Lipid Res. 44 2-3: 125-53. doi:10.1016/j.plipres.2005.04.001. PMID 15893380. ^ Donnelly JG 2001. Folic acid. Crit Rev Clin Lab Sci 38 3: 183-223. doi:10.1080/20014091084209. PMID 11451208. ^ Søballe B, Poole RK 1999. Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology Reading, Engl. 145 Pt 8: 1817-30. PMID 10463148. ^ Linster CL, Van Schaftingen E 2007. Vitamin C. Biosynthesis, recycling and degradation in mammals. FEBS J. 274 1: 1-22. doi:10.1111/j.1742-4658.2006.05607.x. PMID 17222174. ^ Mack M, Grill S 2006. Riboflavin analogs and inhibitors of riboflavin biosynthesis. Appl. Microbiol. Biotechnol. 71 3: 265-75. doi:10.1007/s00253-006-0421-7. PMID 16607521. ^ Knowles JR 1980. Enzyme-catalyzed phosphoryl transfer reactions. Annu. Rev. Biochem. 49: 877-919. doi:10.1146/annurev.bi.49.070180.004305. PMID 6250450. ^ 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. ^ Negishi M, Pedersen LG, Petrotchenko E, et al 2001. Structure and function of sulfotransferases. Arch. Biochem. Biophys. 390 2: 149-57. doi:10.1006/abbi.2001.2368. PMID 11396917. ^ Crane FL 2001. Biochemical functions of coenzyme Q10. Journal of the American College of Nutrition 20 6: 591-8. PMID 11771674. ^ Thony B, Auerbach G, Blau N 2000. Tetrahydrobiopterin biosynthesis, regeneration and functions. Biochem J 347 Pt 1: 1-16. doi:10.1042/0264-6021:3470001. PMID 10727395. ^ Buchanan; Gruissem, Jones 2000. Biochemistry molecular biology of plants, 1st ed., American society of plant physiology. ISBN 0-943088-39-9. ^ Ginsburg V 1978. Comparative biochemistry of nucleotide-linked sugars. Prog. Clin. Biol. Res. 23: 595-600. PMID 351635. ^ Grill D, Tausz T, De Kok LJ 2001. Significance of glutathione in plant adaptation to the environment. Springer. ISBN 1402001789. ^ Meister A, Anderson ME 1983. Glutathione. Annu. Rev. Biochem. 52: 711-60. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189. ^ Taylor CD, Wolfe RS 1974. Structure and methylation of coenzyme MHSCH2CH2SO3. J. Biol. Chem. 249 15: 4879-85. PMID 4367810. ^ Balch WE, Wolfe RS 1979. Specificity and biological distribution of coenzyme M 2-mercaptoethanesulfonic acid. J. Bacteriol. 137 1: 256-63. PMID 104960. ^ 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. doi:10.1073/pnas.83.12.4238. PMID 3086878. ^ Vorholt JA, Thauer RK 1997. The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 248 3: 919-24. doi:10.1111/j.1432-1033.1997.00919.x. PMID 9342247. ^ DiMarco AA, Bobik TA, Wolfe RS 1990. Unusual coenzymes of methanogenesis. Annu. Rev. Biochem. 59: 355-94. doi:10.1146/annurev.bi.59.070190.002035. PMID 2115763. ^ Chen X, Li N, Ellington AD 2007. Ribozyme catalysis of metabolism in the RNA world. Chem. Biodivers. 4 4: 633-55. doi:10.1002/cbdv.200790055. PMID 17443876. ^ Koch A 1998. How did bacteria come to be?. Adv Microb Physiol 40: 353-99. PMID 9889982. ^ Ouzounis C, Kyrpides N 1996. The emergence of major cellular processes in evolution. FEBS Lett 390 2: 119-23. doi:10.1016/0014-57939600631-X. PMID 8706840. ^ White HB 1976. Coenzymes as fossils of an earlier metabolic state. J. Mol. Evol. 7 2: 101-4. doi:10.1007/BF01732468. PMID 1263263. ^ Saran D, Frank J, Burke DH 2003. The tyranny of adenosine recognition among RNA aptamers to coenzyme A. BMC Evol. Biol. 3: 26. doi:10.1186/1471-2148-3-26. PMID 14687414. ^ Jadhav VR, Yarus M 2002. Coenzymes as coribozymes. Biochimie 84 9: 877-88. doi:10.1016/S0300-90840201404-9. PMID 12458080. ^ Denessiouk KA, Rantanen VV, Johnson MS 2001. Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins. Proteins 44 3: 282-91. doi:10.1002/prot.1093. PMID 11455601. ^ Harden A, Young WJ. The Alcoholic Ferment of Yeast-Juice Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character Vol. 78, No. 526 Oct., 1906, pp. 369-375 ^ Fermentation of sugars and fermentative enzymes: Nobel Lecture, May 23, 1930. Nobel Foundation. Retrieved on 2007-09-30. ^ Lohmann, K. 1929 Ãœber die Pyrophosphatfraktion im Muskel. Naturwissenschaften 17, 624-625. ^ Lipmann F 1945. Acetylation of sulfanilamide by liver homogenates and extracts. J. Biol. Chem. 160 1: 173-190. ^ Warburg O, Christian W. 1936. Pyridin, the hydrogen-transferring component of the fermentation enzymes pyridine nucleotide. Biochemische Zeitschrift 287: 291. ^ Kalckar HM 1974. Origins of the concept oxidative phosphorylation. Mol. Cell. Biochem. 5 1-2: 55-63. doi:10.1007/BF01874172. PMID 4279328. ^ Lipmann F, 1941. Metabolic generation and utilization of phosphate bond energy. Adv Enzymol 1: 99-162. ^ Friedkin M, Lehninger AL. 1949. Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen. J. Biol. Chem. 178 2: 611-23. PMID 18116985. External links Examples at City University of New York Overview at National Institutes of Health MeSH Coenzymes v d e Proteins: enzymes Topics Active site - Allosteric regulation - Binding site - Catalytically perfect enzyme - Coenzyme - Cofactor - Cooperativity - EC number Enzyme catalysis - Enzyme inhibitor - Enzyme kinetics - Lineweaver-Burk plot - Michaelis-Menten kinetics - List of enzymes Types EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/list v d e Enzyme cofactors Coenzymes vitamins: NAD+ B3 | NADP+ B3 | Coenzyme A B5 | THF / H4F B9, DHF, MTHF | Ascorbic acid C | Menaquinone K | Coenzyme F420 non-vitamins: ATP | CTP | SAM | PAPS | GSH | Coenzyme B | Coenzyme M | Coenzyme Q | Methanofuran | BH4 | H4MPT Organic prosthetic groups vitamins: TPP / ThDP B1 | FMN, FAD B2 | PLP / P5P B6 | Biotin B7 | Methylcobalamin, Cobamamide B12 non-vitamins: Haem / Heme | Lipoic acid | Molybdopterin | PQQ Metal prosthetic groups Ca2+ | Cu2+ | Fe2+, Fe3+ | Mg2+ | Mn2+ | Mo | Ni2+ | Se | Zn2+ Major families of biochemicals Saccharides | Carbohydrates | Glycosides | | Amino acids | Peptides | Proteins | Glycoproteins | | Lipids | Terpenes | Steroids | Carotenoids Alkaloids | Nucleobases | Nucleic acids | | Enzyme cofactors | Flavonoids | Polyketides | Tetrapyrroles Retrieved from http://en..org/wiki/Coenzyme Categories: Coenzymes | Enzymes | Organic compounds | Cofactors Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages العربية Català Česky Dansk Deutsch Español Esperanto Ù?ارسی Français Galego Italiano עברית Lietuvių Nederlands 日本語 Occitan Polski Português РуÑ?Ñ?кий Suomi Svenska Türkçe ä¸æ–‡ This page was last modified on 8 September 2008, at 06:55
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