Galactosyl transferases in mycobacterial cell wall synthesis

J Bacteriol. 2008 Feb;190(3):1141-5. doi: 10.1128/JB.01326-07. Epub 2007 Nov 30.

Abstract

Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis, the Mycobacterium tuberculosis Rv3782 ortholog known to be involved in the initial steps of galactan formation, harbors dual beta-(1-->4) and beta-(1-->5) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Galf-Galf, serves as a direct substrate for full polymerization catalyzed by another bifunctional Galf transferase, GlfT2, the Rv3808c enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Wall / metabolism*
  • Galactans / chemistry
  • Galactans / metabolism*
  • Galactosyltransferases / genetics
  • Galactosyltransferases / metabolism*
  • Humans
  • Mycobacterium smegmatis / enzymology*
  • Mycobacterium smegmatis / genetics
  • Mycobacterium smegmatis / metabolism
  • Mycobacterium tuberculosis / enzymology
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Galactans
  • Recombinant Proteins
  • Galactosyltransferases