Evidence for a novel glycinamide ribonucleotide transformylase in Escherichia coli.
We demonstrate here that Escherichia coli synthesizes two different glycinamide ribonucleotide (GAR) transformylases, both catalyzing the third step in the purine biosynthetic pathway. One is coded for by the previously described purN gene (GAR transformylase N), and a second, hitherto unknown, enzyme is encoded by the purT gene (GAR transformylase T). Mutants defective in the synthesis of the purN- and the purT-encoded enzymes were isolated. Only strains defective in both genes require an exogenous purine source for growth. Our results suggest that both enzymes may function to ensure normal purine biosynthesis. Determination of GAR transformylase T activity in vitro required formate as the C1 donor. Growth of purN mutants was inhibited by glycine. Under these conditions GAR accumulated. Addition of purine compounds or formate prevented growth inhibition. The regulation of the level of GAR transformylase T is controlled by the PurR protein and hypoxanthine.
Institute of Biological Chemistry B, University of Copenhagen, Denmark.
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P
Nygaard
J M
JM
Smith
D000217:Acyltransferases / Q000032:analysis / Q000235:genetics*; D000596:Amino Acids / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D005561:Formates / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial / Q000235:genetics; D005998:Glycine / Q000378:metabolism; D019877:Hydroxymethyl and Formyl Transferases; D007527:Isoenzymes / Q000235:genetics*; D051026:Phosphoribosylglycinamide Formyltransferase; D011687:Purines / Q000378:metabolism
D000596:Amino Acids; D029968:Escherichia coli Proteins; D005561:Formates; D007527:Isoenzymes; D011687:Purines; D019877:Hydroxymethyl and Formyl Transferases; C494825:purT protein, E coli; D051026:Phosphoribosylglycinamide Formyltransferase; D000217:Acyltransferases; D005998:Glycine