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The 3 substrates of this enzyme are ATP, succinate, and CoA, whereas its 3 products are ADP, phosphate, and succinyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is succinate:CoA ligase (ADP-forming).
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".
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]
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. ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. [1] [2] It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. [3] [4] Improper ADP-ribosylation has been implicated in some forms of cancer. [5]
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 ...
The ANT4 protein is a mitochondrial ADP/ATP carrier that catalyzes the exchange of ADP and ATP between the mitochondrial matrix and cytoplasm during ATP synthesis. [6] In addition, ANT4 stabilizes the mitochondrial membrane potential and decreases the permeability transition pore complex (PTPC) opening in order to prevent nuclear chromatin fragmentation and resulting cell death. [7]
ADP-ribose is a protein-glycating agent, and excess levels of ADP-ribose in the cell can cause non-enzymatic ADP-ribosylation. Non-enzymatic ADP-ribosylation can inactivate protein targets that contain nucleotide-binding sites when the adenylate moiety of ADP-ribose binds to them, and it can also interfere with metabolic regulation that occurs ...