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Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.

AbstractBACKGROUND:
Mycobacterium tuberculosis is a pathogenic prokaryote adapted to survive in hostile environments. In this organism and other Gram-positive actinobacteria, the metabolic pathways of glycogen and trehalose are interconnected.
RESULTS:
In this work we show the production, purification and characterization of recombinant enzymes involved in the partitioning of glucose-1-phosphate between glycogen and trehalose in M. tuberculosis H37Rv, namely: ADP-glucose pyrophosphorylase, glycogen synthase, UDP-glucose pyrophosphorylase and trehalose-6-phosphate synthase. The substrate specificity, kinetic parameters and allosteric regulation of each enzyme were determined. ADP-glucose pyrophosphorylase was highly specific for ADP-glucose while trehalose-6-phosphate synthase used not only ADP-glucose but also UDP-glucose, albeit to a lesser extent. ADP-glucose pyrophosphorylase was allosterically activated primarily by phosphoenolpyruvate and glucose-6-phosphate, while the activity of trehalose-6-phosphate synthase was increased up to 2-fold by fructose-6-phosphate. None of the other two enzymes tested exhibited allosteric regulation.
CONCLUSIONS:
Results give information about how the glucose-1-phosphate/ADP-glucose node is controlled after kinetic and regulatory properties of key enzymes for mycobacteria metabolism.
GENERAL SIGNIFICANCE:
This work increases our understanding of oligo and polysaccharides metabolism in M. tuberculosis and reinforces the importance of the interconnection between glycogen and trehalose biosynthesis in this human pathogen.
AuthorsMatías D Asención Diez, Ana M Demonte, Karl Syson, Diego G Arias, Andrii Gorelik, Sergio A Guerrero, Stephen Bornemann, Alberto A Iglesias
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1850 Issue 1 Pg. 13-21 (Jan 2015) ISSN: 0006-3002 [Print] Netherlands
PMID25277548 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2014. Published by Elsevier B.V.
Chemical References
  • Bacterial Proteins
  • Glucosephosphates
  • Recombinant Proteins
  • Glucose-6-Phosphate
  • Glycogen
  • Trehalose
  • glucose-1-phosphate
  • Glucosyltransferases
  • Glycogen Synthase
  • trehalose-6-phosphate synthase
  • Glucose-1-Phosphate Adenylyltransferase
  • UTP-Glucose-1-Phosphate Uridylyltransferase
Topics
  • Allosteric Regulation
  • Bacterial Proteins (genetics, metabolism)
  • Glucose-1-Phosphate Adenylyltransferase (genetics, metabolism)
  • Glucose-6-Phosphate (metabolism)
  • Glucosephosphates (metabolism)
  • Glucosyltransferases (genetics, metabolism)
  • Glycogen (biosynthesis)
  • Glycogen Synthase (genetics, metabolism)
  • Kinetics
  • Metabolic Networks and Pathways
  • Models, Biological
  • Mycobacterium tuberculosis (enzymology, metabolism)
  • Recombinant Proteins (metabolism)
  • Substrate Specificity
  • Trehalose (biosynthesis)
  • UTP-Glucose-1-Phosphate Uridylyltransferase (genetics, metabolism)

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