Coenzyme 81654 223549388 2008-07-04T15:49:36Z Dryphi 6577659 At the end of the intro section, added link to "ATP" and improved appearance of link to "NAD+" with superscript "+". [[Image:CoenzymeA.png|thumb|250px|Coenzyme A]] '''Coenzymes''' are small [[organic compound|organic]] non-[[protein]] [[molecule]]s that carry chemical groups between [[enzyme]]s.<ref>{{cite web |url=http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#33 |title=Glossary of Terms Used in Bioinorganic Chemistry: Coenzymes |accessdate=2007-10-30 |last=de Bolster |first=M.W.G. |date=1997 |publisher=International Union of Pure and Applied Chemistry}}</ref> Coenzymes are sometimes referred to as ''cosubstrates''. These molecules are [[Substrate (biochemistry) |substrate]]s for enzymes and do not form a permanent part of the enzymes' structures. This distinguishes coenzymes from [[prosthetic group]]s, which are non-protein components that are bound tightly to enzymes - such as [[iron-sulfur protein|iron-sulfur centers]], [[flavin]] or [[haem]] groups. Both coenzymes and prosthetic groups are types of the broader group of [[cofactor (biochemistry)|cofactors]], which are any non-protein molecules (usually organic molecules or metal ions) that are required by an enzyme for its activity.<ref>{{cite web |url=http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#34 |title=Glossary of Terms Used in Bioinorganic Chemistry: Cofactors |accessdate=2007-10-30 |last=de Bolster |first=M.W.G. |date=1997 |publisher=International Union of Pure and Applied Chemistry}}</ref> 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|coenzyme Q<sub>10</sub>]] and [[nicotinamide adenine dinucleotide]] (NAD<sup>+</sup>). 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 [[phosphorylation|phosphorylate]] [[adenosine diphosphate]] (ADP), converting it into ATP, while enzymes such as [[kinase]]s dephosphorylate the ATP and convert it back to ADP. Coenzymes molecules are often [[vitamin]]s or are made from vitamins. Many coenzymes contain the [[nucleotide]] [[adenosine]] as part of their structures, such as [[Adenosine_triphosphate|ATP]], [[coenzyme A]] and [[NAD%2B|NAD<sup>+</sup>]]. This common structure may reflect a common evolutionary origin as part of [[ribozyme]]s in an ancient [[RNA world]]. ==Coenzymes as metabolic intermediates== [[Image:NAD oxidation reduction.svg|thumb|right|250px|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 group]]s.<ref>{{cite journal |author=Mitchell P |title=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 |journal=Eur J Biochem |volume=95 |issue=1 |pages=1-20 |year=1979 |pmid=378655 | doi = 10.1111/j.1432-1033.1979.tb12934.x }}</ref> This common chemistry allows cells to use a small set of metabolic intermediates to carry chemical groups between different reactions.<ref>{{cite journal |author=Wimmer M, Rose I |title=Mechanisms of enzyme-catalyzed group transfer reactions |journal=Annu Rev Biochem |volume=47 |issue= |pages=1031-78 |year= |pmid=354490 | doi = 10.1146/annurev.bi.47.070178.005123 }}</ref> 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 [[dehydrogenase]]s that use [[nicotinamide adenine dinucleotide]] (NADH) as a cofactor. Here, hundreds of separate types of enzymes remove electrons from their substrates and [[redox|reduce]] NAD<sup>+</sup> to NADH. This reduced coenzyme is then a substrate for any of the [[reductase]]s in the cell that need to reduce their substrates.<ref name=Pollak>{{cite journal |author=Pollak N, Dölle C, Ziegler M |title=The power to reduce: pyridine nucleotides--small molecules with a multitude of functions |journal=Biochem. J. |volume=402 |issue=2 |pages=205-18 |year=2007 |pmid=17295611 |url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17295611 | doi = 10.1042/BJ20061638 }}</ref> 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&nbsp;[[Mole (unit)|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&nbsp;moles of ATP daily which is around 50 to 75&nbsp;kg. Typically, a human will use up their body weight of ATP over the course of the day.<ref name="Di Carlo">Di Carlo, S. E. and Coliins, H. L. (2001) [http://advan.physiology.org/cgi/content/full/25/2/70 "Estimating ATP resynthesis during a marathon run: a method to introduce metabolism"] Advan. Physiol. Edu. 25: 70-71. </ref> This means that each ATP molecule is recycled 1000 to 1500 times daily. ==Types== Acting as coenzymes in organisms is the major role of [[vitamin]]s, although vitamins do have other functions in the body.<ref>{{cite journal |author=Bolander FF |title=Vitamins: not just for enzymes |journal=Curr Opin Investig Drugs |volume=7 |issue=10 |pages=912–5 |year=2006 |pmid=17086936}}</ref> Coenzymes are also commonly made from [[nucleotide]]s: 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 [[methanogen]]s, which are restricted to this group of [[archaea]].<ref>{{cite journal |author=Rouvière PE, Wolfe RS |title=Novel biochemistry of methanogenesis |journal=J. Biol. Chem. |volume=263 |issue=17 |pages=7913–6 |year=1988 |pmid=3131330 |url=http://www.jbc.org/cgi/reprint/263/17/7913}}</ref> ===Vitamins and derivatives=== {| class="wikitable" | '''Coenzyme''' || '''Vitamin''' || '''Additional component''' || '''Chemical group(s) transferred''' || '''Distribution''' |- | [[Nicotinamide adenine dinucleotide|NAD<sup>+</sup>]] and [[Nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]]&nbsp;<ref name=Pollak/> || [[Niacin]] (B<sub>3</sub>) || ADP || [[Electron]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- | [[Coenzyme A]]&nbsp;<ref>{{cite journal |author=Leonardi R, Zhang YM, Rock CO, Jackowski S |title=Coenzyme A: back in action |journal=Prog. Lipid Res. |volume=44 |issue=2-3 |pages=125–53 |year=2005 |pmid=15893380 |doi=10.1016/j.plipres.2005.04.001}}</ref> || [[Pantothenic acid]] (B<sub>5</sub>) || ADP || [[Acetyl|Acetyl group]] and other [[acyl|acyl groups]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- | [[Tetrahydrofolic acid]]&nbsp;<ref>{{cite journal |author=Donnelly JG |title=Folic acid |journal=Crit Rev Clin Lab Sci |volume=38 |issue=3 |pages=183–223 |year=2001 |pmid=11451208 |doi=10.1080/20014091084209}}</ref> || [[Folic acid]] (B<sub>9</sub>) || [[glutamic acid|Glutamate]] residues || [[Methyl]], [[aldehyde|formyl]], [[methylene]] and formimino groups || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Vitamin K|Menaquinone]]&nbsp;<ref name=Søballe>{{cite journal |author=Søballe B, Poole RK |title=Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management |journal=Microbiology (Reading, Engl.) |volume=145 ( Pt 8) |issue= |pages=1817&ndash;30 |year=1999 |pmid=10463148 |url=http://mic.sgmjournals.org/cgi/reprint/145/8/1817.pdf}}</ref> || Vitamin K || None || [[Carbonyl|Carbonyl group]] and [[electron]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Ascorbic acid]]&nbsp;<ref>{{cite journal |author=Linster CL, Van Schaftingen E |title=Vitamin C. Biosynthesis, recycling and degradation in mammals |journal=FEBS J. |volume=274 |issue=1 |pages=1–22 |year=2007 |pmid=17222174 |doi=10.1111/j.1742-4658.2006.05607.x}}</ref> || Vitamin C || None || [[Electron]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Coenzyme F420]]&nbsp;<ref>{{cite journal |author=Mack M, Grill S |title=Riboflavin analogs and inhibitors of riboflavin biosynthesis |journal=Appl. Microbiol. Biotechnol. |volume=71 |issue=3 |pages=265–75 |year=2006 |pmid=16607521 | doi = 10.1007/s00253-006-0421-7 }}</ref> || [[Riboflavin]] (B<sub>2</sub>) || Amino acids || [[Electron]]s || [[Methanogen]]s and some [[bacteria]] |- |} ===Non-vitamins=== {| class="wikitable" | '''Coenzyme''' || '''Chemical group(s) transferred''' || '''Distribution''' |- |[[Adenosine triphosphate]]&nbsp;<ref>{{cite journal |author=Knowles JR |title=Enzyme-catalyzed phosphoryl transfer reactions |journal=Annu. Rev. Biochem. |volume=49 |issue= |pages=877–919 |year=1980 |pmid=6250450 | doi = 10.1146/annurev.bi.49.070180.004305 }}</ref> || [[Phosphate|Phosphate group]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[S-Adenosyl methionine]]&nbsp;<ref>{{cite journal |author=Chiang P, Gordon R, Tal J, Zeng G, Doctor B, Pardhasaradhi K, McCann P |title=S-Adenosylmethionine and methylation |journal=FASEB J |volume=10 |issue=4 |pages=471–80 |year=1996 |pmid=8647346}}</ref> || [[Methyl group]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[3'-Phosphoadenosine-5'-phosphosulfate]]&nbsp;<ref>{{cite journal |author=Negishi M, Pedersen LG, Petrotchenko E, ''et al'' |title=Structure and function of sulfotransferases |journal=Arch. Biochem. Biophys. |volume=390 |issue=2 |pages=149–57 |year=2001 |pmid=11396917 | doi = 10.1006/abbi.2001.2368 }}</ref> || [[Sulfate|Sulfate group]] || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- | [[Coenzyme Q]]&nbsp;<ref>{{cite journal |author=Crane FL |title=Biochemical functions of coenzyme Q10 |journal=Journal of the American College of Nutrition |volume=20 |issue=6 |pages=591&ndash;8 |year=2001 |pmid=11771674 |url=http://www.jacn.org/cgi/content/full/20/6/591}}</ref> || [[Electron]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Tetrahydrobiopterin]]&nbsp;<ref>{{cite journal | author=Thony B, Auerbach G, Blau N | title=Tetrahydrobiopterin biosynthesis, regeneration and functions | journal=Biochem J | year=2000 | pages=1–16 | volume=347 Pt 1 |pmid=10727395 |url=http://www.pubmedcentral.gov/articlerender.fcgi?tool=pubmed&pubmedid=10727395 | doi=10.1042/0264-6021:3470001}}</ref> || [[Oxygen]] atom and [[electron]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Cytidine triphosphate]]&nbsp;<ref name=Plantbiochemistry>{{cite book |last= Buchanan |coauthors= Gruissem, Jones |title= Biochemistry & molecular biology of plants |edition=1st ed. |publisher= American society of plant physiology|year=2000 |isbn=0-943088-39-9}}</ref> || [[Diacylglycerol]]s and lipid head groups || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Nucleotide sugar]]s&nbsp;<ref name=Ginsburg>{{cite journal |author=Ginsburg V |title=Comparative biochemistry of nucleotide-linked sugars |journal=Prog. Clin. Biol. Res. |volume=23 |issue= |pages=595–600 |year=1978 |pmid=351635}}</ref> || [[Monosaccharide]]s || [[Bacteria]], [[archaea]] and [[eukaryote]]s |- |[[Glutathione]]&nbsp;<ref>{{cite book | title=Significance of glutathione in plant adaptation to the environment| url=http://books.google.com/books?hl=sv&lr=&id=aX2eJf1i67IC&oi=fnd&pg=PA13&ots=8feo-QOEPa&sig=XAMjZ0Wan17vmoUKg_FFNRl8g0I#PPP1,M1| author=Grill D, Tausz T, De Kok LJ| date=2001| publisher=Springer| isbn=1402001789}}</ref><ref>{{cite journal |author=Meister A, Anderson ME |title=Glutathione |journal=Annu. Rev. Biochem. |volume=52 |issue= |pages=711–60 |year=1983 |pmid=6137189 | doi = 10.1146/annurev.bi.52.070183.003431 }}</ref> || [[Electron]]s || Some [[bacteria]] and most [[eukaryote]]s |- | [[Coenzyme M]]&nbsp;<ref>{{cite journal |author=Taylor CD, Wolfe RS |title=Structure and methylation of coenzyme M(HSCH2CH2SO3) |journal=J. Biol. Chem. |volume=249 |issue=15 |pages=4879–85 |year=1974 |pmid=4367810 |url=http://www.jbc.org/cgi/reprint/249/15/4879}}</ref><ref>{{cite journal |author=Balch WE, Wolfe RS |title=Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid) |journal=J. Bacteriol. |volume=137 |issue=1 |pages=256–63 |year=1979 |pmid=104960 |url=http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=218444&blobtype=pdf}}</ref> || [[Methyl group]] || [[Methanogen]]s |- |[[Coenzyme B]]&nbsp;<ref>{{cite journal |author=Noll KM, Rinehart KL, Tanner RS, Wolfe RS |title=Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue=12 |pages=4238–42 |year=1986 |pmid=3086878 |url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3086878 | doi = 10.1073/pnas.83.12.4238 }}</ref> || [[Electron]]s || [[Methanogen]]s |- |[[Methanofuran]]&nbsp;<ref>{{cite journal |author=Vorholt JA, Thauer RK |title=The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea |journal=Eur. J. Biochem. |volume=248 |issue=3 |pages=919–24 |year=1997 |pmid=9342247 | doi = 10.1111/j.1432-1033.1997.00919.x }}</ref> || [[aldehyde|Formyl group]] || [[Methanogen]]s |- |[[Tetrahydromethanopterin]]&nbsp;<ref>{{cite journal |author=DiMarco AA, Bobik TA, Wolfe RS |title=Unusual coenzymes of methanogenesis |journal=Annu. Rev. Biochem. |volume=59 |issue= |pages=355–94 |year=1990 |pmid=2115763 | doi = 10.1146/annurev.bi.59.070190.002035 }}</ref> || [[Methyl group]] || [[Methanogen]]s |} ==Evolution== {{further|[[Abiogenesis]]}} Coenzymes, such as [[Adenosine triphosphate|ATP]] and [[NADH]], are present in all known forms of life and form a core part of [[metabolism]]. Such universal [[Conservation (genetics)|conservation]] indicates that these molecules evolved very early in the development of living things.<ref>{{cite journal |author=Chen X, Li N, Ellington AD |title=Ribozyme catalysis of metabolism in the RNA world |journal=Chem. Biodivers. |volume=4 |issue=4 |pages=633–55 |year=2007 |pmid=17443876 | doi = 10.1002/cbdv.200790055 }}</ref> 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.<ref>{{cite journal |author=Koch A |title=How did bacteria come to be? |journal=Adv Microb Physiol |volume=40 |issue= |pages=353–99 |year=1998 |pmid=9889982}}</ref><ref>{{cite journal |author=Ouzounis C, Kyrpides N |title=The emergence of major cellular processes in evolution |journal=FEBS Lett |volume=390 |issue=2 |pages=119-23 |year=1996 |pmid=8706840 | doi = 10.1016/0014-5793(96)00631-X }}</ref> Coenzymes may have been present even earlier in the [[Timeline of evolution|history of life]] on Earth.<ref>{{cite journal |author=White HB |title=Coenzymes as fossils of an earlier metabolic state |journal=J. Mol. Evol. |volume=7 |issue=2 |pages=101–4 |year=1976 |pmid=1263263 | doi = 10.1007/BF01732468 }}</ref> 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 hypothesis|RNA world]], with early [[ribozyme]]s evolving to bind a restricted set of nucleotides and related compounds.<ref>{{cite journal |author=Saran D, Frank J, Burke DH |title=The tyranny of adenosine recognition among RNA aptamers to coenzyme A |journal=BMC Evol. Biol. |volume=3 |issue= |pages=26 |year=2003 |pmid=14687414 |url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=14687414 | doi = 10.1186/1471-2148-3-26 }}</ref><ref>{{cite journal |author=Jadhav VR, Yarus M |title=Coenzymes as coribozymes |journal=Biochimie |volume=84 |issue=9 |pages=877–88 |year=2002 |pmid=12458080 | doi = 10.1016/S0300-9084(02)01404-9 }}</ref> 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 [[protein domain|domain]]s, which had originally evolved to bind a different cofactor.<ref>{{cite journal |author=Denessiouk KA, Rantanen VV, Johnson MS |title=Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins |journal=Proteins |volume=44 |issue=3 |pages=282–91 |year=2001 |pmid=11455601 | doi = 10.1002/prot.1093 }}</ref> This process of adapting a pre-evolved structure for a novel use is referred to as ''[[exaptation]]''. ==History== {{further|[[History of biochemistry]]}} The first coenzyme to be discovered was NAD<sup>+</sup>, which was identified by [[Arthur Harden]] and William Youndin 1906.<ref>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 </ref> 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]].<ref>{{cite web |url=http://nobelprize.org/nobel_prizes/chemistry/laureates/1929/euler-chelpin-lecture.pdf |title=Fermentation of sugars and fermentative enzymes: Nobel Lecture, May 23, 1930 |accessdate=2007-09-30 |publisher=Nobel Foundation}}</ref> Other coenzymes were identified throughout the early 20th century, with ATP being isolated in 1929 by Karl Lohmann,<ref>Lohmann, K. (1929) ''Über die Pyrophosphatfraktion im Muskel.'' Naturwissenschaften 17, 624–625.</ref> and coenzyme A being discovered in 1945 by [[Fritz Albert Lipmann]].<ref>{{cite journal |author=Lipmann F |title=Acetylation of sulfanilamide by liver homogenates and extracts |journal=J. Biol. Chem. |volume=160 |issue=1 |pages=173–190 |year=1945 |url=http://www.jbc.org/cgi/reprint/160/1/173}}</ref> The functions of coenzymes were at first mysterious, but in 1936, [[Otto Heinrich Warburg]] identified the function of NAD<sup>+</sup> in hydride transfer.<ref>{{cite journal |author=Warburg O, Christian W.|title=Pyridin, the hydrogen-transferring component of the fermentation enzymes (pyridine nucleotide) |journal=Biochemische Zeitschrift |volume=287 |year=1936 |pages=291}}</ref> 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.<ref>{{cite journal |author=Kalckar HM |title=Origins of the concept oxidative phosphorylation |journal=Mol. Cell. Biochem. |volume=5 |issue=1–2 |pages=55&ndash;63 |year=1974 |pmid=4279328 | doi = 10.1007/BF01874172 }}</ref> This confirmed the central role of ATP in energy transfer that had been proposed by Fritz Albert Lipmann in 1941.<ref>{{cite journal |author=Lipmann F, |title=Metabolic generation and utilization of phosphate bond energy |journal=Adv Enzymol |volume=1 |pages=99&ndash;162 |year=1941}}</ref> Later, in 1949, Morris Friedkin and [[Albert L. Lehninger]] proved that the coenzyme NAD<sup>+</sup> linked metabolic pathways such as the citric acid cycle and the synthesis of ATP.<ref>{{cite journal |author=Friedkin M, Lehninger AL. |title=Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen |journal=J. Biol. Chem. |volume=178 |issue=2 |pages=611&ndash;23 |year=1949 |url=http://www.jbc.org/cgi/reprint/178/2/611 | pmid = 18116985 }}</ref> ==See also== * [[Cofactor (biochemistry)|Cofactor]] * [[Enzymes]] * [[Adenosine triphosphate]] ==References== {{reflist|2}} ==External links== * [http://academic.brooklyn.cuny.edu/biology/bio4fv/page/coenzy_.htm Examples] at [[City University of New York]] * [http://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=stryer.section.1088 Overview] at [[National Institutes of Health]] * {{MeshName|Coenzymes}} {{Enzymes}} {{Enzyme cofactors}} [[Category:Coenzymes| ]] [[Category:Enzymes]] [[Category:Organic compounds]] [[Category:Cofactors]] [[ca:Coenzim]] [[cs:Koenzym]] [[da:Coenzym]] [[de:Koenzym]] [[es:Coenzima]] [[eo:Koenzimo]] [[fa:کوآنزیم]] [[fr:Coenzyme]] [[gl:Coenzima]] [[it:Cofattore (biologia)]] [[he:קואנזים]] [[nl:Co-enzym]] [[ja:補酵素]] [[pl:Koenzymy]] [[pt:Coenzima]] [[ru:Коферменты]] [[fi:Koentsyymi]] [[sv:Koenzym]] [[tr:Koenzim]] [[zh:辅酶]]