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Adenosine monophosphate
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<h2 id="production-and-degradation">Production and degradation</h2> <p>AMP does not have the high energy <a href="/facts/Phosphoanhydride/fwekhW32">phosphoanhydride</a> bond associated with ADP and ATP. AMP can be produced from <a href="/facts/Adenosine_diphosphate/JEDnsCjn">ADP</a> by the <a href="/facts/Adenylate_kinase/XVLmsCUa">myokinase (adenylate kinase)</a> reaction when the ATP reservoir in the cell is low:<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a><a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p> 2 ADP → ATP + AMP <p>Or AMP may be produced by the <a href="/facts/Hydrolysis/JTvwIHPs">hydrolysis</a> of one <a href="/facts/High_energy_phosphate/fwekhW32">high energy phosphate</a> bond of ADP: </p> ADP + H2O → AMP + <a href="/facts/Phosphate/FDGVCxUG">Pi</a> <p>AMP can also be formed by hydrolysis of <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> into AMP and <a href="/facts/Pyrophosphate/L9FPEkhF">pyrophosphate</a>: </p> ATP + H2O → AMP + <a href="/facts/Pyrophosphate/L9FPEkhF">PPi</a> <p>When RNA is broken down by living systems, nucleoside monophosphates, including adenosine monophosphate, are formed. </p><p>AMP can be regenerated to ATP as follows: </p> AMP + ATP → 2 ADP (adenylate kinase in the opposite direction) ADP + Pi → ATP (this step is most often performed in aerobes by the <a href="/facts/ATP_synthase/5NBMxsVX">ATP synthase</a> during <a href="/facts/Oxidative_phosphorylation/en2l08P9">oxidative phosphorylation</a>) <p>AMP can be converted into <a href="/facts/Inosine_monophosphate/V3IevdQz">inosine monophosphate</a> by the <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> <a href="/facts/Myoadenylate_deaminase/yEnSyISa">myoadenylate deaminase</a>, freeing an <a href="/facts/Ammonia/MtLtJFtz">ammonia</a> group. </p><p>In a <a href="/facts/Catabolism/CFWUdphX">catabolic</a> pathway, the <a href="/facts/Purine_nucleotide_cycle/AWagGvCk">purine nucleotide cycle</a>, adenosine monophosphate can be converted to <a href="/facts/Uric_acid/gPMSfLcT">uric acid</a>, which is excreted from the body in mammals.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h2 id="physiological-role-in-regulation">Physiological role in regulation</h2> <h3>AMP-activated kinase regulation</h3> <p>The eukaryotic cell enzyme <a href="/facts/AMP-activated_protein_kinase/Uka4mXB7">5' adenosine monophosphate-activated protein kinase</a>, or AMPK, utilizes AMP for <a href="/facts/Homeostasis/rloTGAHa">homeostatic</a> energy processes during times of high cellular energy expenditure, such as exercise.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> Since ATP cleavage, and corresponding <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylation</a> reactions, are utilized in various processes throughout the body as a source of energy, ATP production is necessary to further create energy for those mammalian cells. AMPK, as a cellular energy sensor, is activated by decreasing levels of ATP, which is naturally accompanied by increasing levels of ADP and AMP.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> </p><p>Though phosphorylation appears to be the main <a href="/facts/Enzyme_activator/soAFcLGS">activator</a> for AMPK, some studies suggest that AMP is an <a href="/facts/Allosteric_regulation/alMRuyt9">allosteric regulator</a> as well as a <a href="/facts/Agonist/nz8U5NNp">direct agonist</a> for AMPK.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> Furthermore, other studies suggest that the high ratio of AMP:ATP levels in cells, rather than just AMP, activate AMPK.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> For example, the AMP-activated kinases of <i><a href="/facts/Caenorhabditis_elegans/XJVJzPn2">Caenorhabditis elegans</a></i> and <i><a href="/facts/Drosophila_melanogaster/KtnHVCcB">Drosophila melanogaster</a></i> were found to have been activated by AMP, while <a href="/facts/Yeast/eGD24nfI">yeast</a> and plant kinases were not allosterically activated by AMP.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p><p>AMP binds to the <i>γ</i>-subunit of AMPK, leading to the activation of the kinase, and then eventually a <a href="/facts/Cascade_reaction/lWpMYkLM">cascade</a> of other processes such as the activation of <a href="/facts/Catabolism/CFWUdphX">catabolic</a> pathways and <a href="/facts/Enzyme_inhibitor/MkFwGXHJ">inhibition</a> of <a href="/facts/Anabolism/eH3Q5AHF">anabolic</a> pathways to regenerate ATP. Catabolic mechanisms, which generate ATP through the release of energy from breaking down molecules, are activated by the AMPK enzyme while anabolic mechanisms, which utilize energy from ATP to form products, are inhibited.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> Though the <i>γ-</i>subunit can bind AMP/ADP/ATP, only the binding of AMP/ADP results in a conformational shift of the enzyme protein. This variance in AMP/ADP versus ATP binding leads to a shift in the <a href="/facts/Dephosphorylation/WkeXmpgs">dephosphorylation</a> state for the enzyme.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> The dephosphorylation of AMPK through various protein <a href="/facts/Phosphatase/LBJs1fXx">phosphatases</a> completely inactivates catalytic function. AMP/ADP protects AMPK from being inactivated by binding to the <i>γ</i>-subunit and maintaining the dephosphorylation state.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> </p> <h2 id="camp">cAMP</h2> <p class="note">Main article: <a href="/facts/Cyclic_AMP/flK2vwUe">Cyclic AMP</a></p> <p>AMP can also exist as a cyclic structure known as <a href="/facts/Cyclic_adenosine_monophosphate/flK2vwUe">cyclic AMP</a> (or cAMP). Within certain cells the enzyme <a href="/facts/Adenylate_cyclase/WnCSuV96">adenylate cyclase</a> makes cAMP from ATP, and typically this reaction is regulated by hormones such as <a href="/facts/Adrenaline/k7vvMI7E">adrenaline</a> or <a href="/facts/Glucagon/NVEnH03n">glucagon</a>. cAMP plays an important role in intracellular signaling.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> In skeletal muscle, cyclic AMP, triggered by adrenaline, starts a cascade (<a href="/facts/CAMP-dependent_pathway/3ARkSDYn">cAMP-dependent pathway</a>) for the conversion of myophosphorylase-b into the phosphorylated form of <a href="/facts/Myophosphorylase/D3eFMdow">myophoshorylase</a>-a for glycogenolysis.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/DNA/nB89Iauz">DNA</a></li> <li><a href="/facts/Oligonucleotide/Gc99fPnC">Oligonucleotide</a></li> <li><a href="/facts/Phosphodiesterase/zRdFKnKH">Phosphodiesterase</a></li> <li><a href="/facts/Glutamate_flavoring/337RzmDQ">Glutamate flavoring</a></li> <li><a href="/facts/Kikunae_Ikeda/RdmFCgdE">Kikunae Ikeda</a></li> <li><a href="/facts/Umami/H3otVQWf">Umami</a></li> <li><a href="/facts/Ajinomoto/e5tUHjaP">Ajinomoto</a></li> <li><a href="/facts/Tien_Chu_Ve-Tsin/n8hctX7L">Tien Chu Ve-Tsin</a></li> <li><a href="/facts/Glutamic_acid/7oXbNcvu">Glutamic acid</a></li> <li><a href="/facts/Disodium_glutamate/xQPPyYnq">Disodium glutamate</a></li> <li><a href="/facts/Monopotassium_glutamate/16MJD2GX">Monopotassium glutamate</a></li> <li><a href="/facts/Disodium_inosinate/UCLkA8zT">Disodium inosinate</a></li> <li><a href="/facts/Guanosine_monophosphate/ex8VI4dR">Guanosine monophosphate</a></li> <li><a href="/facts/Inosinic_acid/V3IevdQz">Inosinic acid</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Ming D, Ninomiya Y, Margolskee RF (August 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22308">"Blocking taste receptor activation of gustducin inhibits gustatory responses to bitter compounds"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 96 (17): 9903–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1999PNAS...96.9903M">1999PNAS...96.9903M</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.96.17.9903">10.1073/pnas.96.17.9903</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22308">22308</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10449792">10449792</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="http://gmd.mpimp-golm.mpg.de/Spectrums/661B03AA-D8B1-4A01-9CEA-6BCEF0E7B15C.aspx">GMD MS Spectrum</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"Adenosine monophosphate (Compound)". PubChem. NCBI. Retrieved 30 April 2020. <a href="https://pubchem.ncbi.nlm.nih.gov/compound/Adenosine-monophosphate" target="_blank">https://pubchem.ncbi.nlm.nih.gov/compound/Adenosine-monophosphate</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>"Nomenclature of Carbohydrates: (Recommendations 1996)". Journal of Carbohydrate Chemistry. 16 (8): 1191–1280. 1997. doi:10.1080/07328309708005748. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Jauker M, Griesser H, Richert C (November 2015). "Spontaneous Formation of RNA Strands, Peptidyl RNA, and Cofactors". Angewandte Chemie. 54 (48): 14564–9. doi:10.1002/anie.201506593. PMC 4678511. PMID 26435376. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678511" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678511</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"Adenosine monophosphate". The Human Metabolome Database. Retrieved 3 July 2020. <a href="https://hmdb.ca/metabolites/HMDB0000045" target="_blank">https://hmdb.ca/metabolites/HMDB0000045</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Baker, Julien S.; McCormick, Marie Clare; Robergs, Robert A. (2010). "Interaction among Skeletal Muscle Metabolic Energy Systems during Intense Exercise". Journal of Nutrition and Metabolism. 2010: 905612. doi:10.1155/2010/905612. ISSN 2090-0732. PMC 3005844. 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PMID 21769098. <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>Faubert B, Vincent EE, Poffenberger MC, Jones RG (January 2015). "The AMP-activated protein kinase (AMPK) and cancer: many faces of a metabolic regulator". Cancer Letters. 356 (2 Pt A): 165–70. doi:10.1016/j.canlet.2014.01.018. PMID 24486219. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Hardie DG (15 September 2011). "AMP-activated protein kinase—an energy sensor that regulates all aspects of cell function". Genes & Development. 25 (18): 1895–1908. doi:10.1101/gad.17420111. ISSN 0890-9369. PMC 3185962. 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Retrieved 10 October 2023. <a href="https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/02%3A_Unit_II-_Bioenergetics_and_Metabolism/15%3A_Glucose_Glycogen_and_Their_Metabolic_Regulation/15.03%3A_15.3_Glycogenolyis_and_its_Regulation_by_Glucagon_and_Epinephrine_Signaling" target="_blank">https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/02%3A_Unit_II-_Bioenergetics_and_Metabolism/15%3A_Glucose_Glycogen_and_Their_Metabolic_Regulation/15.03%3A_15.3_Glycogenolyis_and_its_Regulation_by_Glucagon_and_Epinephrine_Signaling</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> </ol>