This Article Full Text Full Text (PDF) Other Versions of this Article: JB.01326-07v1 190/3/1141    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Belánová, M. Articles by Mikusová, K. PubMed PubMed Citation Articles by Belánová, M. Articles by Mikusová, K.

Galactosyl Transferases in Mycobacterial Cell Wall Synthesis

Martina Beláová,¹ Petronela Dianiková,¹ Patrick J. Brennan,^2* Gladys C. Completo,³ Natisha L. Rose,³ Todd L. Lowary,³ and Katarína Mikuová^1*

Department of Biochemistry, Comenius University, Faculty of Natural Sciences, Bratislava, Slovakia SK-842 15,¹ Mycobacterial Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado 80523,² Alberta Ingenuity Centre for Carbohydrate Science and Department of Chemistry, The University of Alberta, Edmonton, Alberta, Canada T6G 2G2³

Received 15 August 2007/ Accepted 17 November 2007

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 β-(14) and β-(15) 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.

Published ahead of print on 30 November 2007.