Highly efficient chemoenzymatic synthesis of beta1-4-linked galactosides with promiscuous bacterial beta1-4-galactosyltransferases

Chem Commun (Camb). 2010 Sep 7;46(33):6066-8. doi: 10.1039/c0cc01381a. Epub 2010 Jul 12.

Abstract

Two bacterial beta1-4-galactosyltransferases, NmLgtB and Hp1-4GalT, exhibit promiscuous and complementary acceptor substrate specificity. They have been used in an efficient one-pot multienzyme system to synthesize LacNAc, lactose, and their derivatives including those containing negatively charged 6-O-sulfated GlcNAc and C2-substituted GlcNAc or Glc, from monosaccharide derivatives and inexpensive Glc-1-P.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Galactosides / chemical synthesis*
  • Galactosides / chemistry
  • Helicobacter pylori / enzymology*
  • N-Acetyllactosamine Synthase / chemistry*
  • N-Acetyllactosamine Synthase / genetics
  • Neisseria meningitidis / enzymology*
  • Pasteurella multocida / enzymology*
  • Recombinant Fusion Proteins / chemistry*
  • Recombinant Fusion Proteins / genetics
  • Substrate Specificity

Substances

  • Galactosides
  • Recombinant Fusion Proteins
  • N-Acetyllactosamine Synthase