adenosine-kinase and purine
adenosine-kinase has been researched along with purine* in 3 studies
Reviews
2 review(s) available for adenosine-kinase and purine
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Purine Salvage Pathway in Mycobacterium tuberculosis.
Millions of deaths worldwide are caused by the aetiological agent of tuberculosis, Mycobacterium tuberculosis. The increasing prevalence of this disease, the emergence of drug-resistant strains, and the devastating effect of human immunodeficiency virus coinfection have led to an urgent need for the development of new and more efficient antimycobacterial drugs. The modern approach to the development of new chemical compounds against complex diseases, especially the neglected endemic ones, such as tuberculosis, is based on the use of defined molecular targets. Among the advantages, this approach allows (i) the search and identification of lead compounds with defined molecular mechanisms against a specific target (e.g. enzymes from defined pathways), (ii) the analysis of a great number of compounds with a favorable cost/benefit ratio, and (iii) the development of compounds with selective toxicity. The present review describes the enzymes of the purine salvage pathway in M. tuberculosis as attractive targets for the development of new antimycobacterial agents. Enzyme kinetics and structural data have been included to provide a thorough knowledge on which to base the search for compounds with biological activity. We have focused on the mycobacterial homologues of this pathway as potential targets for the development of new antitubercular agents. Topics: 5'-Nucleotidase; Adenosine Deaminase; Adenosine Kinase; Adenylosuccinate Lyase; Adenylosuccinate Synthase; IMP Dehydrogenase; Mycobacterium tuberculosis; N-Glycosyl Hydrolases; Nucleoside-Phosphate Kinase; Pentosyltransferases; Purine-Nucleoside Phosphorylase; Purines | 2011 |
Enzymes involved in purine metabolism--a review of histochemical localization and functional implications.
Many enzymes are involved in the biosynthesis, interconversion, and degradation of purine compounds. The exact function of these enzymes is still unknown, but they seem to play important roles other than in purine metabolism. To elucidate their functional roles, it is imperative to clarify their tissue distribution at the cellular or subcellular level. The present review summarizes the currently available information about their histochemical localization and proposed functions. In general, 5'-nucleotidase has been considered as a marker enzyme for the plasma membrane, and is considered to be a key enzyme in the generation of adenosine, a potential vasodilator. However, from its wide range of localization in tissues it is also considered to be related to the membrane movement of cells in the transitional epithelium, cellular motile response, transport process, cellular growth, synthesis of fibrous protein and calcification, lymphocyte activation, neurotransmission, and oxygen sensing mechanism. Adenosine deaminase (ADA) is present in all tissues in mammals. Although the main function of ADA is the development of the immune system in humans, it seems to be associated with the differentiation of epithelial cells and monocytes, neurotransmission, and maintenance of gestation. Purine nucleoside phosphorylase (PNP) is generally considered as a cytosolic enzyme, but recently, mitochondrial PNP, a different protein from cytosolic PNP, was reported. PNP is also widely expressed in human tissues. It is found in most tissues of the body, but the highest activity is in peripheral blood granulocyte and lymphoid tissues. It is also related to the development of T-cell immunity in humans as is ADA. Moreover, its contribution to centriole replication and/or regulation of microtubule assembly has been suggested. Immunohistochemical localization of xanthine oxidase has been reported in various tissues from various animal species. Xanthine oxidase has been suggested to be involved in the pathogenesis of post-ischemic reperfusion tissue injury through the generation of reactive oxygen species, while the extensive tissue localization of xanthine dehydrogenase/oxidase suggests several other roles for this enzyme, including a protective barrier against bacterial infection by producing either superoxide radicals or uric acid. Furthermore, an involvement in cellular proliferation and differentiation has been suggested. Urate oxidase is generally considered a liver-specific enzym Topics: 5'-Nucleotidase; Adenine Phosphoribosyltransferase; Adenosine Deaminase; Adenosine Kinase; Amidine-Lyases; Amidohydrolases; AMP Deaminase; Animals; Enzymes; Humans; Hypoxanthine Phosphoribosyltransferase; Purine-Nucleoside Phosphorylase; Purines; Rats; Urate Oxidase; Ureohydrolases; Xanthine Oxidase | 1999 |
Other Studies
1 other study(ies) available for adenosine-kinase and purine
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Adenosine Kinase couples sensing of cellular potassium depletion to purine metabolism.
Adenosine Kinase (ADK) regulates the cellular levels of adenosine (ADO) by fine-tuning its metabolic clearance. The transfer of γ-phosphate from ATP to ADO by ADK involves regulation by the substrates and products, as well as by Mg Topics: Adenosine Kinase; Amino Acids; Binding Sites; Enzyme Activation; Kinetics; Magnetic Resonance Imaging; Metabolic Networks and Pathways; Molecular Conformation; Mutation; Phosphorylation; Potassium; Protein Binding; Purines; Structure-Activity Relationship | 2018 |