Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12

Bioorg Med Chem Lett. 2009 Nov 15;19(22):6429-32. doi: 10.1016/j.bmcl.2009.09.039. Epub 2009 Sep 17.

Abstract

N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report the broad substrate specificity of the pyrophosphorylase domain of GlmU during its uridyltransfer reaction and the substrate priority is ranked in the following order: UTP > dUTP > dTTP >> CTP > dATP/dm(6) ATP. This pyrophosphorylase domain of GlmU is also a tool to synthesize UDP-GlcNAc analogs, two examples of which were synthesized herein in multiple mg scale in vitro.

MeSH terms

  • Acetylglucosamine / analogs & derivatives
  • Binding Sites
  • Escherichia coli K12 / enzymology*
  • Molecular Structure
  • Nucleotides / metabolism
  • Nucleotidyltransferases / metabolism*
  • Phosphates / metabolism
  • Polyphosphates / metabolism*
  • Protein Conformation
  • Substrate Specificity
  • Uridine Triphosphate / metabolism

Substances

  • Nucleotides
  • Phosphates
  • Polyphosphates
  • N-acetylglucosamine-1-phosphate
  • Nucleotidyltransferases
  • UDPacetylglucosamine pyrophosphorylase
  • triphosphoric acid
  • Uridine Triphosphate
  • Acetylglucosamine