Abstract 2351 Kinetic and Thermodynamic Investigation of Glu13 and His40 as a catalytic dyad in F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium tuberculosis

F420-dependent glucose-6-phosphate dehydrogenase (FGD) is an enzyme found in Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis disease. FGD catalyzes the conversion of glucose-6-phosphate (G6P) to 6-phosphogluconolactone, utilizing F420 cofactor as a hydride acceptor. This reaction is important in the production of the reduced F420 cofactor and nucleic acid biosynthesis within Mtb, as well as the development of pharmaceuticals to treat multi-drug resistant and extreme drug-resistant forms of tuberculosis.

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Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109193
Primary Topic
Biochemical and Molecular Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 2351 Kinetic and Thermodynamic Investigation of Glu13 and His40 as a catalytic dyad in F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium tuberculosis

Alaa Aziz, Ghader Bashiri, Kayunta Johnson‐Winters, Edward N. Baker et al.
Journal of Biological Chemistry
Biochemical and Molecular Research
article

Abstract 2351 Kinetic and Thermodynamic Investigation of Glu13 and His40 as a catalytic dyad in F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium tuberculosis

Alaa Aziz, Ghader Bashiri, Kayunta Johnson‐Winters, Edward N. Baker, Lindsay Davis, Ravi Ramkissoon
article en

Abstract

F420-dependent glucose-6-phosphate dehydrogenase (FGD) is an enzyme found in Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis disease. FGD catalyzes the conversion of glucose-6-phosphate (G6P) to 6-phosphogluconolactone, utilizing F420 cofactor as a hydride acceptor. This reaction is important in the production of the reduced F420 cofactor and nucleic acid biosynthesis within Mtb, as well as the development of pharmaceuticals to treat multi-drug resistant and extreme drug-resistant forms of tuberculosis.

Journal of Biological ChemistryVol. 301(5)
The University of Texas at Arlington (US)
National Institutes of Health
Good health and well-being
Openalex Percentile: Top 88%
Biochemical and Molecular Research
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