The structural and mechanistic basis of bacterial sugar nucleotide-modifying enzymes

RA Field, James Henderson Naismith

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

Recently, carbohydrates have come to the fore because of their central role in many biological processes. One area of current interest concerns the enzymatic modification of sugar nucleotides, in relation to both secondary metabolite glycosylation and the formation of complex cell surface-associated glycoconjugates. Bacteria, in particular, have proven to be a rich field in which to study these transformations, because they are often unique to specific classes of organisms. This has led to the realization that such microbial biosynthetic pathways might be exploited in the generation of novel antibiotics, or indeed serve as targets for such compounds. This work illustrates the interplay between protein structure determination, chemistry, and molecular biology in providing insight into the mechanism of such biochemical transformations.

Original languageEnglish
Pages (from-to)7637-7647
Number of pages11
JournalBiochemistry
Volume42
DOIs
Publication statusPublished - 1 Jul 2003

Keywords

  • UDP-N-ACETYLGLUCOSAMINE
  • URIDINE DIPHOSPHOGLUCOSE DEHYDROGENASE
  • DIPHOSPHATE GALACTOSE 4-EPIMERASE
  • ENTERICA SEROVAR TYPHIMURIUM
  • DTDP-GLUCOSE 4,6-DEHYDRATASE
  • GDP-MANNOSE 4,6-DEHYDRATASE
  • L-RHAMNOSE PATHWAY
  • ESCHERICHIA-COLI
  • CRYSTAL-STRUCTURE
  • ACTIVE-SITE

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