[Mechanisms of rat liver thiamine pyrophosphokinase activation by magnesium ions]. 1979

V V Vinogradov, and S A Strumilo

The role of Mg2+ in the activation of thiamine pyrophosphokinase from rat liver was studied. The dependence of the thiamine pyrophosphokinase reaction rate on total and free ATP concentrations suggests that the role of the metal comes down to optimization of conditions of the active enzyme-substrate complex formation due to incorporation of the reactions of Mg2+ and ATP-4 consecutive acception, the affinity of the latter for the enzyme being higher than that of Mg-ATP-2. The kinetic parameters of the reaction were determined. In the absence of ATP-4 free Mg2+ ions were shown to compete with the Mg-ATP-2 complex (Ki = 18 . 10(-3) M). Thiamine pyrophosphokinase is also inhibited by free ATP-4 with Ki = 3 . 10(-3) M.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000255 Adenosine Triphosphate An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013836 Thiamin Pyrophosphokinase An enzyme that catalyzes the formation of thiamine pyrophosphate from ATP and thiamine. EC 2.7.6.2. Thiamine Pyrophosphokinase,Pyrophosphokinase, Thiamin,Pyrophosphokinase, Thiamine
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

V V Vinogradov, and S A Strumilo
March 1979, Biokhimiia (Moscow, Russia),
V V Vinogradov, and S A Strumilo
March 1978, Biokhimiia (Moscow, Russia),
V V Vinogradov, and S A Strumilo
January 1977, Voprosy meditsinskoi khimii,
V V Vinogradov, and S A Strumilo
December 1970, Biochimica et biophysica acta,
V V Vinogradov, and S A Strumilo
December 1976, Biokhimiia (Moscow, Russia),
V V Vinogradov, and S A Strumilo
October 1976, Biokhimiia (Moscow, Russia),
V V Vinogradov, and S A Strumilo
January 1983, Acta vitaminologica et enzymologica,
V V Vinogradov, and S A Strumilo
January 1979, Methods in enzymology,
V V Vinogradov, and S A Strumilo
January 1978, Methods in enzymology,
V V Vinogradov, and S A Strumilo
January 1984, Voprosy meditsinskoi khimii,
Copied contents to your clipboard!