Menu
Home
People
Places
Arts
History
Plants & Animals
Science
Life & Culture
Technology
Reference.org
Prosthetic group
open-in-new
<h2 id="list-of-prosthetic-groups">List of prosthetic groups</h2> <p>The table below contains a list of some of the most common prosthetic groups. </p> <table><tbody><tr><th>Prosthetic group</th><th>Function</th><th>Distribution</th></tr><tr><td><a href="/facts/Flavin_mononucleotide/cWutCJmR">Flavin mononucleotide</a> <a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a></td><td><a href="/facts/Redox/Pyd5RVcj">Redox</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/FAD/uzADx3ES">Flavin adenine dinucleotide</a> <a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a></td><td><a href="/facts/Redox/Pyd5RVcj">Redox</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Pyrroloquinoline_quinone/qlT3mnmp">Pyrroloquinoline quinone</a> <a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a></td><td><a href="/facts/Redox/Pyd5RVcj">Redox</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a></td></tr><tr><td><a href="/facts/Pyridoxal_phosphate/GTGIzISg">Pyridoxal phosphate</a> <a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a></td><td><a href="/facts/Transamination/Ntj23r8y">Transamination</a>, <a href="/facts/Decarboxylation/Uugc18fz">decarboxylation</a> and <a href="/facts/Deamination/aBIhMC23">deamination</a></td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Biotin/WAaVxyB7">Biotin</a> <a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a></td><td><a href="/facts/Carboxylation/8zNzYvnP">Carboxylation</a></td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Methylcobalamin/RzM8TUnv">Methylcobalamin</a> <a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a></td><td><a href="/facts/Methylation/EvDMWVW5">Methylation</a> and <a href="/facts/Isomerisation/sxv23uKl">isomerisation</a></td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Thiamine_pyrophosphate/xGQAGmhC">Thiamine pyrophosphate</a> <a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a></td><td>Transfer of 2-carbon groups, α cleavage</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Heme/fRhyJAAb">Heme</a> <a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a></td><td><a href="/facts/Oxygen/acyn6o8r">Oxygen</a> binding and <a href="/facts/Redox/Pyd5RVcj">redox</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Molybdopterin/AH29dl0c">Molybdopterin</a> <a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a></td><td><a href="/facts/Oxygenase/HCJvvLKP">Oxygenation</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Lipoic_acid/9wTHHWBf">Lipoic acid</a> <a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a></td><td><a href="/facts/Redox/Pyd5RVcj">Redox</a> reactions</td><td><a href="/facts/Bacteria/wC8xSCsU">Bacteria</a>, <a href="/facts/Archaea/Adxh0aHw">archaea</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a></td></tr><tr><td><a href="/facts/Cofactor_F430/A8U27JTt">Cofactor F430</a></td><td><a href="/facts/Methanogenesis/5sA0no5A">Methanogenesis</a></td><td><a href="/facts/Archaea/Adxh0aHw">Archaea</a></td></tr></tbody></table> <h2 id="external-links">External links</h2> <ul><li><a href="http://www.bio.mtu.edu/%7Ehlyoungs/BL4010/cofactors.ppt">Cofactors PowerPoint lecture</a> <a href="https://web.archive.org/web/20161005230343/http://www.bio.mtu.edu/%7Ehlyoungs/BL4010/cofactors.ppt">Archived</a> 2016-10-05 at the <a href="/facts/Wayback_Machine/nmQ3a6JC">Wayback Machine</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>de Bolster, M.W.G. (1997). "Glossary of Terms Used in Bioinorganic Chemistry: Prosthetic groups". International Union of Pure and Applied Chemistry. Archived from the original on 2012-11-28. Retrieved 2007-10-30. <a href="https://web.archive.org/web/20121128194239/http://www.chem.qmul.ac.uk/iupac/bioinorg/PR.html#24" target="_blank">https://web.archive.org/web/20121128194239/http://www.chem.qmul.ac.uk/iupac/bioinorg/PR.html#24</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Metzler DE (2001) Biochemistry. The chemical reactions of living cells, 2nd edition, Harcourt, San Diego. <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Nelson DL and Cox M.M (2000) Lehninger, Principles of Biochemistry, 3rd edition, Worth Publishers, New York <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Campbell MK and Farrell SO (2009) Biochemistry, 6th edition, Thomson Brooks/Cole, Belmont, California <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Joosten V, van Berkel WJ (2007). "Flavoenzymes". Curr Opin Chem Biol. 11 (2): 195–202. doi:10.1016/j.cbpa.2007.01.010. PMID 17275397. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Joosten V, van Berkel WJ (2007). "Flavoenzymes". Curr Opin Chem Biol. 11 (2): 195–202. doi:10.1016/j.cbpa.2007.01.010. PMID 17275397. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature. 280 (5725): 843–4. Bibcode:1979Natur.280..843S. doi:10.1038/280843a0. PMID 471057. S2CID 3094647.{{cite journal}}: CS1 maint: multiple names: authors list (link) PMID 471057 <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Eliot AC, Kirsch JF (2004). "Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations". Annu. Rev. Biochem. 73: 383–415. doi:10.1146/annurev.biochem.73.011303.074021. PMID 15189147. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Jitrapakdee S, Wallace JC (2003). "The biotin enzyme family: conserved structural motifs and domain rearrangements". Curr. Protein Pept. Sci. 4 (3): 217–29. doi:10.2174/1389203033487199. PMID 12769720. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Banerjee R, Ragsdale SW (2003). "The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes". Annu. Rev. Biochem. 72: 209–47. doi:10.1146/annurev.biochem.72.121801.161828. PMID 14527323. S2CID 37393683. <a href="https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1458&context=biochemfacpub" target="_blank">https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1458&context=biochemfacpub</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Frank RA, Leeper FJ, Luisi BF (2007). "Structure, mechanism and catalytic duality of thiamine-dependent enzymes". Cell. Mol. Life Sci. 64 (7–8): 892–905. doi:10.1007/s00018-007-6423-5. PMC 11136255. PMID 17429582. S2CID 20415735.{{cite journal}}: CS1 maint: multiple names: authors list (link) <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136255" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136255</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Wijayanti N, Katz N, Immenschuh S (2004). "Biology of heme in health and disease". Curr. Med. Chem. 11 (8): 981–6. doi:10.2174/0929867043455521. PMID 15078160.{{cite journal}}: CS1 maint: multiple names: authors list (link) <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Mendel RR, Hänsch R (2002). "Molybdoenzymes and molybdenum cofactor in plants". J. Exp. Bot. 53 (375): 1689–98. doi:10.1093/jxb/erf038. PMID 12147719. <a href="https://doi.org/10.1093%2Fjxb%2Ferf038" target="_blank">https://doi.org/10.1093%2Fjxb%2Ferf038</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Mendel RR, Bittner F (2006). "Cell biology of molybdenum". Biochim. Biophys. Acta. 1763 (7): 621–35. doi:10.1016/j.bbamcr.2006.03.013. PMID 16784786. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH (1998). "Alpha-lipoic acid in liver metabolism and disease". Free Radic. Biol. Med. 24 (6): 1023–39. doi:10.1016/S0891-5849(97)00371-7. PMID 9607614.{{cite journal}}: CS1 maint: multiple names: authors list (link) <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> </ol>