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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.
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.
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In enzymology, an ADP-specific phosphofructokinase (EC 2.7.1.146) is an enzyme that catalyzes the chemical reaction. ADP + D-fructose 6-phosphate AMP + D-fructose 1,6-bisphosphate. Thus, the two substrates of this enzyme are ADP and D-fructose 6-phosphate, whereas its two products are AMP and D-fructose 1,6-bisphosphate.
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]).