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Published October 1, 2006 | Published
Journal Article Open

PurF-Independent Phosphoribosyl Amine Formation in yjgF Mutants of Salmonella enterica Utilizes the Tryptophan Biosynthetic Enzyme Complex Anthranilate Synthase-Phosphoribosyltransferase

Abstract

In Salmonella enterica, the biosynthetic pathways for the generation of purines and the essential cofactor thiamine pyrophosphate branch after sharing five enzymatic steps. Phosphoribosyl amine (PRA) is the first intermediate in the common portion of the pathway and is generated from phosphoribosylpyrophosphate and glutamine by the PurF enzyme (phosphoribosylpyrophosphate amidotransferase). A null mutation in yjgF allows PurF-independent PRA formation by an unknown mechanism. The tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase, composed of the TrpD and TrpE proteins, was shown to be essential for PRA formation in strains lacking both yjgF and purF. The activity generating PRA in a yjgF mutant background has features that distinguish it from the TrpDE-mediated PRA formation shown previously for this enzyme in strains with an active copy of yjgF. The data presented here are consistent with a model in which the absence of YjgF uncovers a new catalytic activity of TrpDE.

Additional Information

© 2006, American Society for Microbiology. Received 24 May 2006/ Accepted 24 July 2006 This work was supported by NIH competitive grant GM47296 to D.M.D. Funds were also provided from a 21st Century Scientists Scholars Award from the J.M. McDonnell fund to D.M.D. We acknowledge the assistance of Inna Larsen in the preparation of the manuscript.

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August 22, 2023
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