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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
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.
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]).
Paris Aéroport, formerly Aéroports de Paris (ADP), is the passenger brand subsidiary of Groupe ADP which operated the airports of Paris and its region, including Paris–Charles de Gaulle, Paris–Orly and Paris–Le Bourget.
Adenosine diphosphate ribose (ADPR) is an ester molecule formed into chains by the enzyme poly ADP ribose polymerase. [1] ADPR is created from cyclic ADP-ribose (cADPR) by the CD38 enzyme using nicotinamide adenine dinucleotide (NAD +) as a cofactor. [1] ADPR binds to and activates the TRPM2 ion channel. [2] ADPR is the most potent agonist of ...
The transporter is an obligate exchange translocase specific for ATP and ADP. It functions to take up ATP from the eukaryotic cell cytoplasm into the bacterium in exchange for ADP. The ATP/ADP uniporters can also transport inorganic phosphate, but not ribonucleoside and monophosphates, as well as deoxyribonucleotides. [3] [4]
(ADP-ribosyl)hydrolase 3 (ARH3) is an enzyme that in humans is encoded by the ADPRHL2 gene (also called ADPRS). This enzyme reverses the proteins’ post-translational addition of ADP-ribose to serine residues as part of the DNA damage response The enzyme is also known to cleave poly(ADP-ribose) polymers, 1''-O-acetyl-ADP-ribose and alpha-NAD +
Further reading. Moss J, Stanley SJ, Oppenheimer NJ (1979). "Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes".
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