Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens

Folia Microbiol (Praha). 1979;24(3):205-10. doi: 10.1007/BF02926449.

Abstract

Differential centrifugation, precipitation with ammonium sulphate and chromatography on DEAE-cellulose led to a twenty-fold purification of glucosyltransferase from Streptomyces aureofaciens B 96. The Michaelis constants for glucosyluridyl diphosphate (UDP-glucose) was 10.8 microM for 1,2-dihydroxy-9,10-anthraquinone (alizarin) 110 microM; the maximum rate of glucosylation reaction was 5.32 mumol per s per mg protein. The pH optimum was at 7.1; the flat temperature optimum was at 30 degrees C. Using some hydroxy derivatives of 9,10-anthraquinone it was found that the production of glucosides from aglycones with alpha-hydroxyl groups was about 1/8 of the values obtained with beta-hydroxyl substrates. In both types of aglycones the presence of another hydroxyl group led to a higher glucoside production.

MeSH terms

  • Anthraquinones
  • Glucosides
  • Glucosyltransferases / isolation & purification*
  • Glucosyltransferases / metabolism
  • Hydrogen-Ion Concentration
  • Streptomyces aureofaciens / enzymology*
  • Temperature
  • Uridine Diphosphate Glucose

Substances

  • Anthraquinones
  • Glucosides
  • Glucosyltransferases
  • Uridine Diphosphate Glucose