Enzymes required for the biosynthesis of N-formylated sugars

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DOIResolve DOI: http://doi.org/10.1016/j.sbi.2016.04.003
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TypeArticle
Journal titleCurrent Opinion in Structural Biology
ISSN0959-440X
Volume41
Pages19
AbstractThe N-formyltransferases, also known as transformylases, play key roles in de novo purine biosynthesis where they catalyze the transfer of formyl groups to primary amine acceptors. These enzymes require N¹⁰-formyltetrahydrofolate for activity. Due to their biological importance they have been extensively investigated for many years, and they are still serving as targets for antifolate drug design. Most of our understanding of the N-formyltransferases has been derived from these previous studies. It is now becoming increasingly apparent, however, that N-formylation also occurs on some amino sugars found on the O-antigens of pathogenic bacteria. This review focuses on recent developments in the biochemical and structural characterization of the sugar N-formyltransferases.
Publication date
PublisherElsevier
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
IdentifierS0959440X1630032X
NPARC number23000335
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Record identifier8c3e0b0c-a04f-4695-b41e-2007d5a5db2e
Record created2016-07-07
Record modified2016-07-07
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