Journal
JOURNAL OF BACTERIOLOGY
Volume 190, Issue 3, Pages 1141-1145Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01326-07
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Funding
- FIC NIH HHS [R03 TW006487] Funding Source: Medline
- NIAID NIH HHS [R01 AI018357, R37 AI018357] Funding Source: Medline
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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 (Gay) 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.
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