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Phosphoribulokinase (PRK) (EC 2.7.1.19) is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle.
In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule.
The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. [1] There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets.
The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases. [2] [3] [4] Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. This functions as an on/off switch for many cellular processes, including metabolism ...
Photosynthesis usually refers to oxygenic photosynthesis, a process that produces oxygen. Photosynthetic organisms store the chemical energy so produced within intracellular organic compounds (compounds containing carbon) like sugars, glycogen , cellulose and starches .
Phosphoglycerate kinase (PGK) deficiency is an X-linked recessive trait associated with hemolytic anemia, mental disorders and myopathy in humans, [16] [17] depending on form – there exists a hemolytic form and a myopathic form. [18]
There are two functions of Nme2 that allow for such regulation; one is the histidine kinase activity, which is the phosphorylation of the channels to regulate what goes through and the other is a scaffold function of the formation of caveolae. The depletion of Nme2/caveolin interaction exhibited a decreased rate of cardiac contractility. [18]
Protein tyrosine kinase plays a role in this task, too. A protein tyrosine kinase called pp125, also referred to as focal adhesion kinase (FAK) is likely at hand in the influence of cellular focal adhesions, as indicated by an immunofluorescent localization of FAK. Focal adhesions are macromolecular structures that function in the transmission ...