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.
Maenpaa P.H., 1984: Poly amines and heparin do not appreciably influence phosphorylation of chromatin proteins hmg 14 and hmg 17 by nuclear protein kinase ii. Biochimica Et Biophysica Acta: 122-127 Phosphorylation of acidic substrates such as casein and phosvitin by nuclear protein kinase Ii is stimulated by polyamines and inhibited by heparin, which mimics an [...]
Endo H., 1982: Poly amines alter the substrate preference of nuclear protein kinase n ii. Biochemistry: 2632-2637 An investigation of the effects of polyamines on substrate specificity of cAMP independent nuclear protein kinase Nii showed that the substrate preference of Nii was drastically altered in the presence of polyamines. When casein was used as a [...]
Williams Ashman H.G., 1983: Poly amine like effects of cobalt iii hexa ammine on various cyclic nucleotide independent protein phospho kinase reactions. Biochemical & Biophysical Research Communications: 139-146 The chemically inert trivalent ion cobalt hexaammine, Co3+(Nh3)6, exerted polyamine-like effects in enhancing certain cyclic nucleotide-independent protein kinase reactions catalyzed by nuclear enzyme preparations from rat ventral [...]
Pollak A., 1979: Poly acrylamide gel entrapment of adenylate kinase and acetate kinase. Journal Of Molecular Catalysis: 177-198 Factors that limit the stability of adenylate kinase and acetate kinase in solution were examined and compared with those that determine stability under conditions encountered during photochemically initiated polymer gel formation in solutions of acrylamide and N,N’-methylenebisacrylamide. [...]
Garcia, E.; Gomez, A.; Ronda, C.; Escarmis, C.; Lopez, R., 1983: Pneumococcal bacterio phage cp 1 contains a protein bound to the 5 termini of its dna. Virology 128(1): 92-104 The genome of the pneumococcal bacteriophage Cp-1 was isolated as a Dna-protein complex. The transfecting activity of this complex is destroyed by treatment with proteolytic [...]
Gergely, P.; Castle, A. G.; Crawford, N., 1980: Platelet phosphorylase kinase ec 126.96.36.199 activity and its regulation by the calcium dependent regulatory protein calmodulin. Biochimica et Biophysica Acta 612(1): 50-55 Platelet phosphorylase kinase (ATP:phosphorylase phosphotransferase, Ec 188.8.131.52) was a Ca2+-sensitive enzyme. It had 2 Ka values for Ca2+, i.e., 0.25 and 2.6.mu.M, respectively. The Ca-dependent [...]
Garland, W.; Dennis, D. T., 1980: Plastid and cytosolic phospho fructo kinase ec 184.108.40.206 from the developing endosperm of ricinus communis comparison of the kinetic and regulatory properties of the iso enzymes. Archives of Biochemistry and Biophysics 204(1): 310-317 A steady-state kinetic analysis of plastid phosphofructokinase at pH 8.2 is consistent with the enzyme having [...]
Sander, B. J.; Lowery, M. S.; Kruckeberg, W. C., 1982: Plasmodium berghei acid insensitive phospho fructo kinase ec 220.127.116.11 in infected mouse erythrocytes. Experimental Parasitology 53(1): 11-16 The rate of glucose utilization by red blood cells infected with P. berghei was not inhibited by an acidic pH which completely inhibited normal red cell glucose consumption. [...]
Bethell I.L., 1979: Plasma protein and red cell enzyme groups among the nepalese. Human Heredity: 14-26 Nepalese blood samples were tested for 2 plasma proteins and 7 red cell enzyme systems. Polymorphic variation was present for the haptoglobin protein system and for the acid phosphatase, phosphoglucomutase locus 1, adenylate kinase and 6-phosphogluconate dehydrogenase loci controlling [...]
Thornley W.R., 1985: Plasma membrane atpase of sugar beta vulgaris beet. Phytochemistry (oxford): 2797-2802 A membrane fraction enriched with magnesium-dependent ATPase activity was isolated from sugarbeet (Beta vulgaris L.) taproot by a combination of differential centrifugation, extraction with Ki and sucrose density gradient centrifugation. This activity was inhibited by vanadate, N,N’-dicyclohexylcarbodiimide and diethylstilbestrol, but was [...]