NDLI: The Role of Gene Duplication in the Evolution of Purine Nucleotide Salvage Pathways

Content Provider	Springer Nature Link
Author	Becerra, Arturo Lazca, Antonio
Copyright Year	1998
Abstract	Purine nucleotides are formed de novo by a widespread biochemical route that may be of monophyletic origin, or are synthesized from preformed purine bases and nucleosides through different salvage pathways. Three monophyletic sets of purine salvage enzymes, each of which catalyzes mechanistically similar reactions, can be identified: (a) adenine-, xanthine-, hypoxanthine- and guanine-phosphoribosyltransferases, which are all homologous among themselves, as well as to nucleoside phosphorylases; (b) adenine deaminase, adenosine deaminase, and adenosine monophophate deaminase; and (c) guanine reductase and inosine monophosphate dehydrogenase. These homologies support the idea that substrate specificity is the outcome of gene duplication, and that the purine nucleotide salvage pathways were assembled by a patchwork process that probably took place before the divergence of the three cell domains (Bacteria, Archaea, and Eucarya). Based on the ability of adenine PRTase to catalyze the condensation of PRPP with 4-aminoimidazole-5-carboxamide (AICA), a simpler scheme of purine nucleotide biosynthesis is presented. This hypothetical route requires the prior evolution of PRPP biosynthesis. Since it has been argued that PRPP, nucleosides, and nucleotides are susceptible to hydrolysis, they are very unlikely prebiotic compounds. If this is the case, it implies that many purine salvage pathways appeared only after the evolution of phosphorylated sugar biosynthetic pathways made ribosides available.
Starting Page	539
Ending Page	553
Page Count	15
File Format	PDF
ISSN	01696149
Journal	Origins of Life and Evolution of Biospheres
Volume Number	28
Issue Number	4-6
e-ISSN	15730875
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	Organic Chemistry Geochemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Ecology, Evolution, Behavior and Systematics Space and Planetary Science

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