In the field of biochemistry, a kinase is a kind of enzyme that has the ability to transfer phosphate groups from donor molecules with high energy levels (such as adenosine triphosphate or ATP) to specific substrates. This chemical process is known as phosphorylation. Belonging to the larger family of phosphotransferases, kinases should not be confused with phosphorylases, which in turn carry out phosporolysis or the breaking of a chemical bond with an inorganic phosphate group. Kinases should also not be confused with phosphatases, which remove phosphate groups from substrates.
There are many kinds of kinases, but the largest of these groups are the protein kinases. This kind of kinases acts on and modify the activity of specific proteins. Kinases are often used to transmit signals and control various complex processes in the cells. Because of their enormous diversity and their important role in signalling, makes them an interesting object of study for scientists. In human bodies alone, scientists have discovered more than five hundred different kinases.
Kinases are also found to act on small molecules such as amino acids, carbohydrates, lipids, and nucleotides, where they play an important role in signalling for various cellular processes or to prime them for metabolic pathways. When naming kinases, scientists often name the substances after their substrates.
Protein kinases modify other proteins through chemically adding phosphate groups to these substances through the process of phosphorylation. This process results into a functional change of the target protein (or the substrate) through changing enzyme activity, cellular location, or the association with other proteins. Kinases also constitute two percent of all human genes, and can also modify up to thirty percent of all human proteins. Protein kinases can also be found in bacteria and plants.
This category contains scientific information on kinase, which are essential enzymes in humans, animals, plants, and bacteria.
Pribilla O., 1980: Frequencies of red cell enzyme polymorphism in the acid phosphatase adenosine deaminase adenylate kinase 6 phospho gluconate dehydrogenase phospho gluco mutase 1 and esterase d systems determined by parallel investigations of turks and germans living in the lubeck area west germany. Zeitschrift Fuer Rechtsmedizin: 55-62 Gene frequencies for red cell enzyme alleles [...]
Markus, M.; Plesser, T., 1983: Free energy dissipation of the pyruvate kinase ec 18.104.22.168 reaction has a minimum at cell metabolite concentrations. Biophysical Chemistry 18(4): 349-352 The ratio of substrates and products (mass action ratio) for the reaction catalyzed by the enzyme pyruvate kinase is measured under the constraint of constant reaction rate for pyruvate [...]
Cox J.A., 1983: Free energy coupling in the interactions between calcium calmodulin and phosphorylase kinase. Journal Of Biological Chemistry3: 14733-14739 Interactions between Ca2+, exogenous calmodulin, and white skeletal muscle phosphorylase kinase have been quantitatively studied by equilibrium gel filtrations and analyzed by means of the so-called linked functions theory. Four moles of calmodulin, each saturated [...]
Watson K.F., 1979: Fractionation of 2 protein kinases from avian myeloblastosis virus and characterization of the protein kinase activity preferring basic phospho acceptor proteins. Journal Of Virology: 872-880 Two protein kinase activities were fractionated from purified virions of avian myeloblastosis virus. Distinguishing characteristics of these 2 protein kinases included their binding properties during purification by [...]
Ahmed K., 1983: Fractionation and partial purification of rat liver nuclear protein kinases. International Journal Of Biochemistry: 1109-1118 Several rat liver nuclear protein kinases were fractionated and partialy purified by utilizing endogenous (nonhistone proteins) and exogenous acidic (dephosphophosvitin) and basic (lysine-rich histone) protein substrates. Three enzymes were active towards endogenous substrates, 2 towards dephosphophosvitin and [...]
“Both G.W., 1987: Fowlpox virus thymidine kinase nucleotide sequence and relationships to other thymidine kinases. Virology: 355-365 The thymidine kinase (Tk) gene of fowlpox virus (Fpv) is located in a 2.2-kb HindIII-ClaI fragment derived from a 5.5-kb EcoR1 fragment of the Fpv genome. The Tk gene was mapped to the region of a 700-bp XbaI [...]
Gupta R.S., 1983: Formycin b resistant mutants of chinese hamster ovary cells novel genetic and biochemical phenotype affecting adenosine kinase. Molecular & Cellular Biology: 1468-1477 Stable mutants which are approximately 3- and 8-fold resistant to the pyrazolopyrimidine nucleosides formycin A and formycin B (FomR) were selected in a single step from mutagenized Chinese hamster ovary [...]
Scott C.R., 1980: Formycin b purine nucleoside phosphorylase and lymphocyte function. Immunological Communications: 257-268 A genetic deficiency of purine nucleoside phosphorylase (Np) is associated with immune dysfunction that specifically affects T cells. An absence of adenosine deaminase (Ada), the preceding enzyme in the pathway of purine recycling, is associated with failure of both T and [...]
Belzer S.K., 1987: Forms of pp 60v src isolated from rous sarcoma virus transformed cells. Journal Of Virology: 1593-1601 It has previously been shown that an electrophoretic variant form of the Rous sarcoma virus transforming protein, pp60v-srv, exists in src-transformed cells. This variant, which was readily observed in vanadate-treated cells, was characterized as possessing extensive [...]
Bowien B., 1981: Formation of enzymes of autotrophic metabolism during heterotrophic growth of alcaligenes eutrophus. Journal Of General Microbiology: 69-78 A. eutrophus strain H16 formed key enzymes of autotrophic metabolism during heterotrophic growth. The formation of the soluble and membrane-bound hydrogenases, ribulose-5-phosphate kinase and ribulosebisphosphate carboxylase, were investigated. Selected enzymes shared by autotrophic and heterotrophic [...]