Open Access Articles- Top Results for Adenosine diphosphate

Adenosine diphosphate

Adenosine diphosphate
Skeletal formula of ADP
Ball-and-stick model of ADP (shown here as a 3- ion)
colspan=2 style="background:#f8eaba; border-top:2px solid transparent; border-bottom:2px solid transparent; text-align:center;" #REDIRECTmw:Help:Magic words#Other
This page is a soft redirect. Names

#REDIRECTmw:Help:Magic words#Other
This page is a soft redirect.-

IUPAC name
[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphono hydrogen phosphate
Other names
adenosine 5′-diphosphate
colspan=2 style="background:#f8eaba; border-top:2px solid transparent; border-bottom:2px solid transparent; text-align:center;" #REDIRECTmw:Help:Magic words#Other
This page is a soft redirect. Identifiers#REDIRECTmw:Help:Magic words#Other
This page is a soft redirect.-

58-64-0 7pxY
ChEBI CHEBI:16761 7pxY
ChEMBL ChEMBL14830 7pxY
ChemSpider 5800 7pxY
DrugBank DB03431 7pxN
EC number 218-249-0
IUPHAR ligand 1712
Jmol-3D images Image
KEGG C00008 7pxN
PubChem Template:Chembox PubChem/format
RTECS number AU7467000
colspan=2 style="background:#f8eaba; border-top:2px solid transparent; border-bottom:2px solid transparent; text-align:center;" #REDIRECTmw:Help:Magic words#Other
This page is a soft redirect. Properties

#REDIRECTmw:Help:Magic words#Other
This page is a soft redirect.-

Molar mass 427.201 g/mol
Appearance white powder
Density 2.49 g/mL
Boiling point Script error: No such module "convert".
log P -2.640
colspan=2 style="background:#f8eaba; border-top:2px solid transparent; border-bottom:2px solid transparent; text-align:center;" #REDIRECTmw:Help:Magic words#Other
This page is a soft redirect. Hazards

#REDIRECTmw:Help:Magic words#Other
This page is a soft redirect.-

Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
 14pxN verify (what is10pxY/10pxN?)
Infobox references

Adenosine diphosphate (ADP) (Adenosine pyrophosphate (APP)) is an important organic compound in metabolism and is essential to the flow of energy in living cells. A molecule of ADP consists of three important structural components: a sugar backbone attached to a molecule of adenine and two phosphate groups bonded to the 5' carbon atom of ribose. The carbon molecules that make up the ring structure of a sugar can be named in a way that more specifically designates the location of the phosphate and adenosine attachments: The sugar backbone of ADP is known as a pentose sugar and consists of five carbon molecules. The two phosphate groups of ADP are added in series to the 5’ carbon of the sugar backbone, while the adenosine molecule attaches to the 1’ carbon.[1]

The two phosphates in ADP can be correlated with ATP and AMP. ATP consists of three phosphate groups attached in series to the 5’ carbon location, whereas ADP contains two phosphate groups attached to the 5’ position, and AMP contains only one phosphate group attached at the 5’ position. Energy transfer used by all living things is a result of dephosphorylation of ATP by enzymes known as ATPases. The cleavage of a phosphate group from ATP results in the coupling of energy to metabolic reactions and a by-product, a molecule of ADP.[1] Being the "molecular unit of currency", ATP is continually being formed from lower-energy molecules of ADP and AMP. The biosynthesis of ATP is achieved throughout processes such as substrate-level phosphorylation, oxidative phosphorylation, and photophosphorylation, all of which facilitating the addition of a phosphate group to an ADP molecule.


ADP-ATP cycling supplies the energy needed to do work in a biological system, the thermodynamic process of transferring energy from one source to another. There are two types of energy: potential energy and kinetic energy. Potential energy can be thought of as stored energy, or usable energy that is available to do work. Kinetic energy is the energy of an object as a result of its motion. The significance of ATP is in its ability to store potential energy within the phosphate bonds. The energy stored between these bonds can then be transferred to do work. For example, the transfer of energy from ATP to the protein myosin causes a conformational change when connecting to actin during muscle contraction. It takes multiple reactions between myosin and actin to effectively produce one muscle contraction, and, therefore, the availability of large amounts of ATP is required to produce each muscle contraction. For this reason, biological processes have evolved to produce efficient ways to replenishment the potential energy of ATP from ADP.[2]

Breaking one of ATP’s phosphorus bonds generates approximately 30.5 kilojoules per Mole of ATP (7.3 kcal).[3] ADP can be converted, or powered back to ATP through the process of releasing the chemical energy available in food; in humans, this is constantly performed via aerobic respiration in the mitochondria.[2] Plants use photosynthetic pathways to convert and store energy from sunlight, also conversion of ADP to ATP.[3] Animals use the energy released in the breakdown of glucose and other molecules to convert ADP to ATP, which can then be used to fuel necessary growth and cell maintenance.[2]

Cellular respiration


The ten-step catabolic pathway of glycolysis is the initial phase of free-energy release in the breakdown of glucose and can be split into two phases, the preparatory phase and payoff phase. ADP and phosphate are needed as precursors to synthesize ATP in the payoff reactions of the TCA cycle and oxidative phosphorylation mechanism.[4] During the payoff phase of glycolysis, the enzymes phosphoglycerate kinase and pyruvate kinase facilitate the addition of a phosphate group to ADP by way of substrate-level phosphorylation.[5]

File:Glycolysis overview.svg
Glycolysis overview


Main article: glycolysis

Glycolysis is performed by all living organisms and consists of 10 steps. The net reaction for the overall process of glycolysis is: Glucose + 2NAD+ + 2 Pi + 2 ADP = 2 pyruvate + 2 ATP + 2 NADH + 2 H2O.[6] Steps 1 and 3 require the input of energy derived from the hydrolysis of ATP to ADP and Pi (inorganic phosphate), whereas steps 7 and 10 require the input of an ADP molecule, each yielding an ATP molecule.[7] The enzymes necessary to break down glucose are found in the cytoplasm, the viscous fluid that fills living cells, where the glycolytic reactions take place.

Citric acid cycle

Main article: citric acid cycle

The citric acid cycle, also known as the Krebs cycle or the TCA (tricarboxylic acid) cycle is an 8-step process that takes the pyruvate generated by glycolysis and generates 4NADH, FADH2, and GTP, which is further converted to ATP.[8] It is only in step 5, where GTP is generated, by succinyl-CoA synthetase, and then converted to ATP, that ADP is used (GTP + ADP → GDP + ATP).[9]

File:Conversion of GTP to ATP.jpg
chemical conversion of GTP to ATP

Oxidative phosphorylation

Oxidative phosphorylation produces 26 of the 30 molecules of ATP generated in cellular respiration by transferring electrons from NADH or FADH2 to O2 through electron carriers.[10] The energy released when electrons are passed from higher-energy NADH or FADH2 to the lower-energy O2 is required to phosphorylate ADP and once again generate ATP.[11] It is this energy coupling and phosphorylation of ADP to ATP that gives the electron transport chain the name oxidative phosphorylation.

Mitochondrial ATP synthase complex

Main article: ATP synthase

During the initial phases of glycolysis and the TCA cycle, cofactors such as NAD+ donate and accept electrons[12] that aid in the electron transport chain's ability to produce a proton gradient across the inner mitochondrial membrane.[13] The ATP synthase complex exists within the mitochondrial membrane (F0 portion) and protrudes into the matrix (F1portion). The energy derived as a result of the chemical gradient is then used to synthesize ATP by coupling the reaction of inorganic phosphate to ADP in the active site of the ATP synthase enzyme; the equation for this can be written as ADP + Pi → ATP.

Blood platelet activation

Under normal conditions, small disk-shape platelets circulate the blood freely and without interaction with one another. ADP is stored in dense bodies inside blood platelets and is released upon platelet activation. ADP interacts with a family of ADP receptors found on platelets (P2Y1, P2Y12, and P2X1), which leads to platelet activation.[14]

  • P2Y1 receptors initiate platelet aggregation and shape change as a result of interactions with ADP.
  • P2Y12 receptors further amplify the response to ADP and draw forth the completion of aggregation.

ADP in the blood is converted to adenosine by the action of ecto-ADPases, inhibiting further platelet activation via adenosine receptors.

See also


  1. ^ a b Cox, Michael; Nelson, David R.; Lehninger, Albert L (2008). Lehninger principles of biochemistry. San Francisco: W.H. Freeman. ISBN 0-7167-7108-X. 
  2. ^ a b c Nave, C.R. (2005). "Adenosine Triphosphate". Hyper Physics [serial on the Internet]. Georgia State University. 
  3. ^ a b Farabee, M.J. (2002). "The Nature of ATP". ATP and Biological Energy [serial on the Internet]. 
  4. ^ Jensen TE, Richter EA (March 2012). "Regulation of glucose and glycogen metabolism during and after exercise". J. Physiol. (Lond.) 590 (Pt 5): 1069–76. PMC 3381815. PMID 22199166. doi:10.1113/jphysiol.2011.224972. 
  5. ^ Liapounova NA, Hampl V, Gordon PM, Sensen CW, Gedamu L, Dacks JB (December 2006). "Reconstructing the mosaic glycolytic pathway of the anaerobic eukaryote Monocercomonoides". Eukaryotic Cell 5 (12): 2138–46. PMC 1694820. PMID 17071828. doi:10.1128/EC.00258-06. 
  6. ^ Medh, J.D. "Glycolysis" (PDF). CSUN.Edu. Retrieved 3 April 2013. 
  7. ^ Bailey, Regina. "10 Steps of Glycolysis". 
  8. ^ "Citric Acid Cycle" (PDF). Takusagawa’s Note. Retrieved 4 April 2013. 
  9. ^ "Biochemistry" (PDF). 
  10. ^ "Oxidative phosphorylation". W H Freeman, 2002. Retrieved 4 April 2013. 
  11. ^ Medh, J. D. "Electron Transport Chain (Overview)" (PDF). Retrieved 4 April 2013. 
  12. ^ Belenky P, Bogan KL, Brenner C (January 2007). "NAD+ metabolism in health and disease". Trends Biochem. Sci. 32 (1): 12–9. PMID 17161604. doi:10.1016/j.tibs.2006.11.006. 
  13. ^ Murray, Robert F. (2003). Harper's illustrated biochemistry. New York: McGraw-Hill. ISBN 0-07-121766-5. 
  14. ^ Murugappa S, Kunapuli SP (2006). "The role of ADP receptors in platelet function". Front. Biosci. 11: 1977–86. PMID 16368572. doi:10.2741/1939. 

Lua error in Module:Authority_control at line 346: attempt to index field 'wikibase' (a nil value).