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Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis.

Abstract
Mycobacteria synthesize intracellular methylglucose lipopolysaccharides (MGLP) proposed to regulate fatty acid synthesis. Although their structures have been elucidated, the identity of most biosynthetic genes remains unknown. The first step in MGLP biosynthesis is catalyzed by a glucosyl-3-phosphoglycerate synthase (GpgS, Rv1208 in Mycobacterium tuberculosis H37Rv). However, a typical glucosyl-3-phosphoglycerate phosphatase (GpgP, EC3.1.3.70) for dephosphorylation of glucosyl-3-phosphoglycerate to glucosylglycerate, was absent from mycobacterial genomes. We purified the native GpgP from Mycobacterium vanbaalenii and identified the corresponding gene deduced from amino acid sequences by mass spectrometry. The M. tuberculosis ortholog (Rv2419c), annotated as a putative phosphoglycerate mutase (PGM, EC5.4.2.1), was expressed and functionally characterized as a new GpgP. Regardless of the high specificity for glucosyl-3-phosphoglycerate, the mycobacterial GpgP is not a sequence homolog of known isofunctional GpgPs. The assignment of a new function in M. tuberculosis genome expands our understanding of this organism's genetic repertoire and of the early events in MGLP biosynthesis.
AuthorsVítor Mendes, Ana Maranha, Susana Alarico, Milton S da Costa, Nuno Empadinhas
JournalScientific reports (Sci Rep) Vol. 1 Pg. 177 ( 2011) ISSN: 2045-2322 [Electronic] England
PMID22355692 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Lipopolysaccharides
  • Recombinant Proteins
  • Phosphoric Monoester Hydrolases
  • phosphoglycerate phosphatase
Topics
  • Cloning, Molecular
  • Escherichia coli (metabolism)
  • Gene Expression Regulation, Bacterial
  • Genome, Bacterial
  • Lipopolysaccharides (biosynthesis)
  • Mycobacterium (enzymology, genetics)
  • Phosphoric Monoester Hydrolases (genetics, metabolism)
  • Phylogeny
  • Recombinant Proteins (metabolism)
  • Substrate Specificity

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