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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.
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
(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 ]
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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.
ATP is initially bound to myosin. When ATPase hydrolyzes the bound ATP into ADP and inorganic phosphate, myosin is positioned in a way that it can bind to actin. Myosin bound by ADP and P i forms cross-bridges with actin and the subsequent release of ADP and P i releases energy as the power stroke. The power stroke causes actin filament to ...
Poly(ADP-ribosyl)ation is an immediate DNA damage-dependent post-translational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. PARP14 belongs to the superfamily of enzymes that perform this modification (Ame et al., 2004 [PubMed 15273990]).