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The Democratic Alliance for Peace (French: Alliance Démocratique pour la Paix, ADP-MALIBA) is a political party in Mali led by Aliou Boubacar Diallo. History [ edit ] The party was registered on 18 March 2013. [1]
ADP-ribose diphosphatase, in particular, hydrolyzes ADP-ribose into AMP and D-ribose 5-phosphate, both of which are intermediates of central metabolic pathways and therefore are easily reused. Other common names for ADP-ribose diphosphatase include ADP-ribose pyrophosphatase and ADPRase. ADP-ribose is commonly referred to as ADPR.
Cyclic ADP-ribose, frequently abbreviated as cADPR, is a cyclic adenine nucleotide (like cAMP) with two phosphate groups present on 5' OH of the adenosine (like ADP), further connected to another ribose at the 5' position, which, in turn, closes the cycle by glycosidic bonding to the nitrogen 1 (N 1) of the same adenine base (whose position N 9 has the glycosidic bond to the other ribose).
(2) ADP + (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate AMP + phosphate + NADPH This enzyme acts equally well on hydrated NADH and hydrated NADPH. References [ edit ]
ADP-ribose 1′′-phosphate phosphatase (EC 3.1.3.84, POA1, Appr1p phosphatase, Poa1p) is an enzyme with systematic name ADP-D-ribose 1′′-phosphate phosphohydrolase. [1] This enzyme catalyses the following chemical reaction
In enzymology, an acetate—CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction. ATP + acetate + CoA ADP + phosphate + acetyl-CoA. The 3 substrates of this enzyme are ATP, acetate, and CoA, whereas its 3 products are ADP, phosphate, and acetyl-CoA.
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.
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