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[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl dihydrogen phosphate
Adenosine 5'-monophosphate, 5'-Adenylic acid
3D model (JSmol)
|Molar mass||347.22 g/mol|
|Appearance||white crystalline powder|
|Melting point||178 to 185 °C (352 to 365 °F; 451 to 458 K)|
|Boiling point||798.5 °C (1,469.3 °F; 1,071.7 K)|
|Acidity (pKa)||0.9, 3.8, 6.1|
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
|‹See TfM› (what is ‹See TfM› ?)|
Adenosine monophosphate (AMP), also known as 5'-adenylic acid, is a nucleotide. AMP consists of a phosphate group, the sugar ribose, and the nucleobase adenine; it is an ester of phosphoric acid and the nucleoside adenosine. As a substituent it takes the form of the prefix adenylyl-.
Production and degradation
- 2 ADP → ATP + AMP
- ADP + H2O → AMP + Pi
- ATP + H2O → AMP + PPi
When RNA is broken down by living systems, nucleoside monophosphates, including adenosine monophosphate, are formed.
AMP can be regenerated to ATP as follows:
- AMP + ATP → 2 ADP (adenylate kinase in the opposite direction)
- ADP + Pi → ATP (this step is most often performed in aerobes by the ATP synthase during oxidative phosphorylation)
Physiological Role in Regulation
AMP-activated kinase regulation
The eukaryotic cell enzyme 5' adenosine monophosphate-activated protein kinase, or AMPK, utilizes AMP for homeostatic energy processes during times of high cellular energy expenditure, such as exercise. Since ATP cleavage, and corresponding phosphorylation 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.
Though phosphorylation appears to be the main activator for AMPK, some studies suggest that AMP is an allosteric regulator as well as a direct agonist for AMPK. Furthermore, other studies suggest that the high ratio of AMP:ATP levels in cells, rather than just AMP, activate AMPK. For example, the species of Caenorhabditis elegans and Drosophila melanogaster and their AMP-activated kinases were found to have been activated by AMP, while species of yeast and plant kinases were not allosterically activated by AMP.
AMP binds to the γ-subunit of AMPK, leading to the activation of the kinase, and then eventually a cascade of other processes such as the activation of catabolic pathways and inhibition of anabolic 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. Though the γ-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 dephosphorylation state for the enzyme. The dephosphorylation of AMPK through various protein phosphatases completely inactivates catalytic function. AMP/ADP protects AMPK from being inactivated by binding to the γ-subunit and maintaining the dephosphorylation state.
AMP can also exist as a cyclic structure known as cyclic AMP (or cAMP). Within certain cells the enzyme adenylate cyclase makes cAMP from ATP, and typically this reaction is regulated by hormones such as adrenaline or glucagon. cAMP plays an important role in intracellular signaling.
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