Download A History of Biochemistry: Selected Topics in the History of by Albert Neuberger, L. L. M. Van Deenen, Giorgio Semenza PDF

By Albert Neuberger, L. L. M. Van Deenen, Giorgio Semenza

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The level of enzyme was then a function of the initiation of mRNA synthesis in the first step. Of five enzyme systems studied deoxynucleotide kinase was unique in that initiation occurred to a substantial but not maximal degree in the presence of only one nucleoside triphosphate, namely ATP. However, upon addition of UTP initiation was as complete as usually found in the presence of all four nucleoside triphosphates [218]. Natale [219] also found that initiation could be effected by the oligonucleotides, ApApApA, UpUpUpU and ApUpU.

The enzymes catalyzing these two reactions have now been purified and designated as glutamine-PRPP amidotransferase and 5'-phosphoribosyl glycinamide synthetase, respectively. There are, of course, two reactions in which formate is utilized in purine nucleotide biosynthesis. The first of these reactions to be studied was the ring closure of 5'-phosphoribosyl 5-amino-4-imidazole carboxamide (AICAR) with 10-formyl tetrahydrofolate to yield inosinic acid. The cognate base of the above nucleotide had been isolated from E.

These experiments suggest that initiation of transcription of mRNA for group 1 and group 3 enzymes occurs at different promoter sites and that mRNA for group 2 enzymes may be formed in part from either site. The case of deoxynucleotide kinase clearly indicated that it fell into a separate class of early enzyme, possibly the quasi-late variety of delayed early enzyme. However, this designation has been modified recently [209] to distinguish genes expressed late in the early period that either do or do not require the participation of the protein product of gene 55.

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