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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).
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.
The company has its origins as the Dealer Services division of Automatic Data Processing (), which was formed in 1973 after ADP acquired National Inventory Control System, Portland OR (NICS) and Computer System Inc., Cincinnati, OH (CSI) providing computerized Accounting, Financial Reporting, Sales Analysis, Lease Accounting, Parts Inventory Control, Customer Relations, Management Systems for ...
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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 ]
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 ...