Inactivation of fructose-1,6-bisphosphate aldolase prevents optimal co-catabolism of glycolytic and gluconeogenic carbon substrates in Mycobacterium tuberculosis.

Inactivation of fructose-1,6-bisphosphate aldolase prevents optimal co-catabolism of glycolytic and gluconeogenic carbon substrates in Mycobacterium tuberculosis.

Metabolic pathways used by Mycobacterium tuberculosis (Mtb) to establish and maintain infections are important for our understanding of pathogenesis and the development of new chemotherapies. To investigate the role of fructose-1,6-bisphosphate aldolase (FBA), we engineered an Mtb strain in which FB...

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Detaylı Bibliyografya
Asıl Yazarlar: Susan Puckett, Carolina Trujillo, Hyungjin Eoh, Joeli Marrero, John Spencer, Mary Jackson, Dirk Schnappinger, Kyu Rhee, Sabine Ehrt
Materyal Türü: Makale
Dil:English
Baskı/Yayın Bilgisi: Public Library of Science (PLoS) 2014-05-01
Seri Bilgileri:PLoS Pathogens
Online Erişim:http://europepmc.org/articles/PMC4031216?pdf=render

Internet

http://europepmc.org/articles/PMC4031216?pdf=render

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