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Read and write a review of the article: Quantitative Analysis of Purine Nucleotides Indicates That Purinosomes Increase de Novo Purine Biosynthesis [1]

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As purine nucleotides have multiple important roles in all the living organisms, the studies about their production and recycling have great attention in life sciences. They are the units of the nucleic acid structure; they serve as energy molecules and have other important metabolic and signaling roles. There is a pathway for de novo synthesis of purines from 5-phospho-α-D-ribose 1-diphosphate as well as a scavenger pathway that recycles existing nucleotides with hypoxanthine as a precursor. Both pathways include IMP as stable intermediate. It is produced de novo in a 10 step pathway catalyzed by 6 enzymes that were found by the same research group that published this paper to form a multienzyme complex [2]. Such complexes bring great advantages in metabolic pathways. They increase the efficiency of pathways by decreasing distances, cutting down diffusion rates and preventing intermediates loss due to the instability. After proving that these enzymes colocalize, forming structures named purinosomes under low-purine conditions, authors conducted various investigations with the aim to understand the functioning and regulation of purinosomes. They found that the purinosome assembly are regulated by cell signaling, by the pathway of CK2 kinase activation [3] and is under the control of microtubule network [4]. Following these findings, they also showed that assembly and disassembly of purinosome is in correlation with GPCRs activation which is involved in cell signaling pathways that trigger mitosis [5]. Heat shock proteins Hsp90 and Hsp70 were found to colocalize with purinosomes and knockdown experiments indicated that they play important role in the assembly of these structures [6].
After determining the factors regulating the purinosome formation...

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