Deoxyguanosine Kinase
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Deoxyguanosine Kinase
In enzymology, a deoxyguanosine kinase () is an enzyme that catalyzes the chemical reaction :ATP + deoxyguanosine \rightleftharpoons ADP + dGMP Thus, the two substrates of this enzyme are ATP and deoxyguanosine, whereas its two products are ADP and dGMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyguanosine 5'-phosphotransferase. Other names in common use include deoxyguanosine kinase (phosphorylating), (dihydroxypropoxymethyl)guanine kinase, 2'-deoxyguanosine kinase, and NTP-deoxyguanosine 5'-phosphotransferase. This enzyme participates in purine metabolism. Structural studies As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and . Clinical Mutations in this gene have been linked to inherited mitochondrial DNA depletion syndromes, neonatal ...
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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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