Solubilization and properties of UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase from Bacillus coagulans AHU 1366 membranes

J Biochem. 1988 Dec;104(6):985-8. doi: 10.1093/oxfordjournals.jbchem.a122595.


The glucosyltransferase which catalyzes the conversion of GlcNAc-PP-undecaprenol into Glc(beta 1----4)GlcNAc-PP-undecaprenol in the presence of UDP-glucose was solubilized from Bacillus coagulans AHU 1366 membranes by treatment with 0.1% Triton X-100 and partially purified by means of column chromatography on Sephacryl S-300 and DEAE-Sephacel. The final preparation was virtually free from other enzymes involved in the de novo synthesis of teichoic acid. The enzyme had a pH optimum of 6.6-8.0 and a Km value for UDP-glucose of 21 microM. The enzyme required 40 mM MgCl2, 0.6 M KCl, and 0.1% Nonidet P-40 for full activity.

MeSH terms

  • Bacillus / enzymology*
  • Chromatography
  • Glucosyltransferases / isolation & purification*
  • Glucosyltransferases / metabolism
  • Glycolipids
  • Hydrogen-Ion Concentration
  • Kinetics
  • Membranes / enzymology
  • Solubility
  • Substrate Specificity
  • Teichoic Acids / biosynthesis
  • Uridine Diphosphate Glucose
  • Uridine Diphosphate Sugars


  • Glycolipids
  • Teichoic Acids
  • Uridine Diphosphate Sugars
  • N-acetylglucosamine-pyrophosphorylundecaprenol
  • Glucosyltransferases
  • UDP-glucose-N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase
  • Uridine Diphosphate Glucose