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.
Miller, J.; Johnson, M.; Wei, R., 1982: Preparation of creatine kinase mm ec 184.108.40.206 iso enzymes from canine and human tissues. Clinica Chimica Acta 118(1): 67-76 An improved method is described for the purification of creatine kinase-Mm isoenzyme from canine and human skeletal muscle. The purification uses a 50-80% (Nh4)2so4 fractionation, Deae-Sephacel ion exchange chromatography [...]
Mencher, D.; Shouval, D.; Reshef, L., 1979: Premature appearance of hepatic phosphoenol pyruvate carboxy kinase ec 220.127.116.11 in fetal rats not mediated by cyclic amp. European Journal of Biochemistry 102(2): 489-496 Injection of streptozotocin in utero to fetuses elicited a premature appearance of cytosolic hepatic activity of phosphoenolpyruvate carboxykinase. This is due to a precocious [...]
Earnshaw, J. S.; Peh, K. H.; Dodgson, K. S.; Olavesen, A. H.; Gacesa, P., 1985: Preferential uptake of intravenously administered hyaluronidase ec 18.104.22.168 hyalosidase by damaged rat myocardium. Bioscience Reports 5(4): 329-334 The induction of myocardial infarction in rats by ligation of the left-anterior coronary artery was confirmed by measurement of increased plasma levels of [...]
Fischer, P. H.; Murphy, D. G.; Kawahara, R., 1983: Preferential inhibition of 5 tri fluoromethyl 2 deoxy uridine phosphorylation by 5 amino 5 deoxy thymidine in uninfected vs. herpes simplex virus infected cells. Molecular Pharmacology 24(1): 90-96 The cytotoxic effects of 5-trifluoromethyl-2′-deoxyuridine (CF3dUrd) were effectively antagonized by 5′-amino-5′-deoxythymidine (5′-AdThd). The antiproliferative actions of CF3dUrd were [...]
Cassell D.J., 1983: Preferential degradation of the beta subunit of purified insulin receptor effect on insulin binding and protein kinase activities of the receptor. Journal Of Biological Chemistry3: 14456-14460 Collagenase preparations (a mixture of enzymes including collgenase, clostripain and a casein-degrading protease) degraded the.beta. subunit (Mw = 95,000) of the purified insulin receptor into fragments [...]
Lusk, J. A.; Manthorpe, C. M.; Kao-Jen, J.; Wilson, J. E., 1980: Predominance of the cytoplasmic form of brain hexo kinase ec 22.214.171.124 in cultured astrocytes. Journal of Neurochemistry 34(6): 1412-1420 Astrocytes were cultured from neonatal rat brain according to the flask culture procedure of Booher and Sensenbrenner. Approximately 80% of the hexokinase (Atp: D-hexose [...]
Vitseva O.I., 1983: Pre steady state kinetics of atp hydrolysis by chloroplast coupling factor 1 atpase. Biokhimiya: 718-724 The kinetics of reversible inactivation of chloroplast Cf1-ATPase by Mg2+ and Adp was studied. The rate of inactivation obeys the 1st-order equation and is independent of Adp concentration. An analysis of the dependence of the inactivation rate [...]
Pfueller K., 1982: Pre natal development of enzymes regulating pyruvate metabolism in pig liver. Acta Biologica Et Medica Germanica8: 601-608 The gluconeogenic enzymes phosphoenolpyruvate carboxykinase (Pepck) and pyruvate carboxylase (Pc) and the glycolytic enzyme pyruvate kinase (Pk), regulating pyruvate metabolism, were determined in the livers of 71 fetuses, which were delivered of 25 dams on [...]
Farrar W.L., 1988: Potentiation of lymphokine activated killer cell differentiation and lymphocyte proliferation by stimulation of protein kinase c or inhibition of adenylate cyclase. Journal Of Immunology: 208-214 Interleukin 2 (Il-2) stimulated the differentiation of human peripheral blood leukocytes into lymphokine-activated killer cells, as well as Dna synthesis of human T lymphocytes. Both effects of [...]
Becker F.F., 1988: Potassium inhibition of transforming protein p85gag mos and reversal of the transformed phenotype in 6m2 cells. Journal Of Cellular Physiology: 445-452 K+ at high concentrations (52-72 mM hypertonic KCl) has been reported to induce reverse transformation in the 6m2 cell, which is a clone of normal rat kidney cells (Nrk) infected with [...]