Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis
The human pathogen Mycobacterium tuberculosis (Mtb) likely utilizes host fatty acids as a carbon source during infection. Gluconeogenesis is essential for the conversion of fatty acids into biomass. A rate-limiting step in gluconeogenesis is the conversion of fructose 1,6-bisphosphate to fructose 6-...
Main Authors: | Ganapathy, Uday, Marrero, Joeli, Calhoun, Susannah, Eoh, Hyungjin, de Carvalho, Luiz Pedro Sorio, Rhee, Kyu, Ehrt, Sabine |
---|---|
Format: | Online |
Language: | English |
Published: |
Nature Publishing Group
2015
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4535450/ |
Similar Items
-
Inactivation of Fructose-1,6-Bisphosphate Aldolase Prevents Optimal Co-catabolism of Glycolytic and Gluconeogenic Carbon Substrates in Mycobacterium tuberculosis
by: Puckett, Susan, et al.
Published: (2014) -
Glucose Phosphorylation Is Required for Mycobacterium tuberculosis Persistence in Mice
by: Marrero, Joeli, et al.
Published: (2013) -
Triosephosphate Isomerase Is Dispensable In Vitro yet Essential for Mycobacterium tuberculosis To Establish Infection
by: Trujillo, Carolina, et al.
Published: (2014) -
Cell cycle-dependent expression and subcellular localization of fructose 1,6-bisphosphatase
by: Mamczur, Piotr, et al.
Published: (2011) -
The Role of Liver Fructose-1,6-Bisphosphatase in Regulating Appetite and Adiposity
by: Visinoni, Sherley, et al.
Published: (2012)