1960
DOI: 10.1128/mmbr.24.3.309-339.1960
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The Biosynthesis and Interconversion of Purines and Their Derivatives1

Abstract: It is regrettable that the volume of published work has precluded direct reference to the many authors whose works have bearing on the biosynthesis and interconversion of purines.

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Cited by 18 publications
(8 citation statements)
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“…The results obtained agree with those of Pomper (1952) and fit in well with current concepts of the biosynthesis of purine nucleotides from phosphoribosylpyrophosphate (PRPP) and their interconversion (Magasanik and Karibian, 1960;Moat and Friedman, 1960;Fig. 5).…”
Section: Discussionsupporting
confidence: 89%
“…The results obtained agree with those of Pomper (1952) and fit in well with current concepts of the biosynthesis of purine nucleotides from phosphoribosylpyrophosphate (PRPP) and their interconversion (Magasanik and Karibian, 1960;Moat and Friedman, 1960;Fig. 5).…”
Section: Discussionsupporting
confidence: 89%
“…Glutamine phosphoribosyl pyrophosphate amidotransferase is an enzyme encoded by the PPAT gene, and GPAT is the first limiting enzyme in the purine biosynthesis pathway (Moat & Friedman ; Koenigsknecht et al . ).…”
Section: Discussionmentioning
confidence: 99%
“…The only parameter measured in this work for which different results were obtained in the isolated perfused liver and in vivo was the α‐ketoglutarate dehydrogenase activity (Figure ). This enzyme participates in both the regulation of carbon and nitrogen fluxes in the liver besides being a probable redox sensor . It is impossible to infer about the significance of the observed modifications.…”
Section: Discussionmentioning
confidence: 99%
“…Conditions for de novo synthesis are given even in the perfused liver. Synthesis of adenine mononucleotides requires glucose (as a source of ribose 5′‐phosphate) and amino acids . Even in the substrate‐free perfused liver, an increased supply of glucosyl units was available because of the enhanced glycogenolysis.…”
Section: Discussionmentioning
confidence: 99%