The adenylate energy charge is an index used to measure the energy status of
biological cells
The cell is the basic structural and functional unit of life forms. Every cell consists of a cytoplasm enclosed within a membrane, and contains many biomolecules such as proteins, DNA and RNA, as well as many small molecules of nutrients an ...
.
ATP or Mg-ATP is the principal molecule for storing and transferring energy in the cell : it is used for biosynthetic pathways, maintenance of transmembrane gradients, movement, cell division, etc... More than 90% of the ATP is produced by phosphorylation of ADP by the
ATP synthase
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). It is classified under ligases as it changes ADP by the formation ...
.
ATP can also be produced by “
substrate level phosphorylation” reactions (ADP phosphorylation by (1,3)-bisphosphoglycerate, phosphoenolpyruvate, phosphocreatine), by the succinate-CoA ligase and phosphoenolpyruvate carboxylkinase, and by
adenylate kinase
Adenylate kinase ( ECbr>2.7.4.3 (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP). By constantly monitoring phosphate nucleotide levels insid ...
, an enzyme that maintains the three adenine nucleotides in equilibrium (
ATP + AMP <=> 2 ADP).
The energy charge is related to
ATP,
ADP and
AMP #REDIRECT Amp
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concentrations. It was first defined by Atkinson and Walton who found that it was necessary to take into account the concentration of all three nucleotides, rather than just ATP and ADP, to account for the energy status in
metabolism
Metabolism (, from el, μεταβολή ''metabolē'', "change") is the set of life-sustaining chemical reactions in organisms. The three main functions of metabolism are: the conversion of the energy in food to energy available to run cell ...
. Since the adenylate kinase maintains two ADP molecules in equilibrium with one ATP (
2 ADP <=> ATP + AMP), Atkinson defined the adenylate energy charge as:
The energy charge of most cells varies between 0.7 and 0.95
- oscillations in this range are quite frequent. Daniel Atkinson showed that when the energy charge increases from 0.6 to 1.0, the
citrate lyase and
phosphoribosyl pyrophosphate synthetase, two enzymes controlling
anabolic
Anabolism () is the set of metabolic pathways that construct molecules from smaller units. These reactions require energy, known also as an endergonic process. Anabolism is the building-up aspect of metabolism, whereas catabolism is the breaking-do ...
(ATP-demanding) pathways are activated,
while the
phosphofructokinase
Phosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
Function
The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. ...
and the
pyruvate dehydrogenase
Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate.
Pyruvate dehydrogenase is us ...
, two enzymes controlling
amphibolic
The term amphibolic ( grc, ἀμφίβολος, translit=amphibolos, lit=ambiguous, struck on both sides) is used to describe a biochemical pathway that involves both catabolism and anabolism. Catabolism is a degradative phase of metabolism in w ...
pathways (supplying ATP as well as important biosynthetic intermediates) are inhibited He concluded that control of these pathways has evolved to maintain the energy charge within rather narrow limits - in other words, that the energy charge, like the pH of a cell, must be buffered at all times. We now know that most if not all anabolic and catabolic pathways are indeed controlled, directly and indirectly, by the energy charge. In addition to direct regulation of several enzymes by adenyl nucleotides, an AMP-activated protein kinase known as
AMP-K phosphorylates and thereby regulates key enzymes when the energy charge decreases. This results in switching off anabolic pathways while switching on catabolic pathways when AMP increases.
Life depends on an adequate energy charge. If ATP synthesis is momentarily insufficient to maintain an adequate energy charge, AMP can be converted by two different pathways to hypoxanthine and ribose-5P, followed by irreversible oxidation of hypoxanthine to uric acid. This helps to buffer the adenylate energy charge by decreasing the total concentration.
References
Metabolism
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