Guanylate Phosphorylase: The Enzyme that Converts Guanosine Monophosphate to Guanosine Diphosphate
The biochemical process in which guanosine monophosphate (GMP) is converted to guanosine diphosphate (GDP) is essential for cellular metabolism and is catalyzed by the enzyme guanylate phosphorylase (GUP). GUP is responsible for the transfer of the terminal phosphate group of GMP to the triphosphate acceptor, ADP, forming GDP. GUP is found in bacteria, fungi, plants and animals, and is especially important in the synthesis of nucleotides, which are the building blocks of DNA and RNA. In 2016, researchers from the University of California, Los Angeles demonstrated that GUP is regulated by a redox-sensitive mechanism. Specifically, they showed that GUP activity is increased in the presence of oxidizing agents, such as hydrogen peroxide, and decreased in the presence of reducing agents, such as dithiothreitol. This finding was significant because it provided insight into how GUP may be regulated in diverse organisms (Eremenko et al., 2016). In 2020, a study conducted by researchers at the University of North Carolina Chapel Hill showed that a particular variant of GUP is involved in the regulation of the production of cyclic GMP, a key component of the signaling pathways that control cell growth and proliferation (Hazelton et al., 2020). Cont….
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