The function of the 5-hydroxymethyl group of lactose in enzymatic hydrolysis with beta-galactosidase from E. coli

Acta Chem Scand (Cph). 1992 Nov;46(11):1114-21. doi: 10.3891/acta.chem.scand.46-1114.

Abstract

A series of 6-substituted methyl lactoside derivatives together with methyl allolactoside and (6S)-methyl [6-2H]lactoside have been synthesized and characterized by NMR spectroscopy. All compounds were tested as substrates for the enzyme beta-galactosidase from E. coli using progress curve kinetic methology both in single-substrate and competition experiments. The results show that the hydrolysis of methyl lactoside to a large extent takes place through an intramolecular transglycosidation reaction via allolactoside. Furthermore, methyl 6-amino-6-deoxy-D-glucopyranoside proved to be an ihibitor for the enzymatic hydrolysis.

Publication types

  • Comparative Study

MeSH terms

  • Escherichia coli / enzymology*
  • Glycosylation
  • Hydrolysis
  • Kinetics
  • Lactose / analogs & derivatives*
  • Lactose / chemistry
  • Lactose / metabolism
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Structure-Activity Relationship
  • Substrate Specificity
  • beta-Galactosidase / metabolism*

Substances

  • beta-Galactosidase
  • Lactose