Mutagenesis of threonine to serine in the active site of Mycobacterium tuberculosis fructose-1,6-bisphosphatase (Class II) retains partial enzyme activity-Reference-Cited by-同舟云学术

Mutagenesis of threonine to serine in the active site of Mycobacterium tuberculosis fructose-1,6-bisphosphatase (Class II) retains partial enzyme activity

Published:2017-09 Issue: Volume:15 Page:48-54
ISSN:2215-017X
Container-title:Biotechnology Reports
language:en
Short-container-title:Biotechnology Reports

Author:

Bondoc Jasper Marc G.,Wolf Nina M.,Ndichuck Michael,Abad-Zapatero Celerino,Movahedzadeh Farahnaz

Funder

Potts Memorial Foundation

Chicago Biomedical Consortium

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biotechnology

Reference9 articles.

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3. glpX gene of Mycobacterium tuberculosis: heterologous expression, purification, and enzymatic characterization of the encoded fructose 1,6-bisphosphatase II;Gutka;Appl. Biochem. Biotechnol.,2011

4. Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis;Ganapathy;Nat. Commun.,2015

5. Structural and biochemical characterization of the type II fructose-1,6-bisphosphatase GlpX from Escherichia coli;Brown;J. Biol. Chem.,2009

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