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Preliminary Studies on Sugar F420‐dependent glucose‐6‐phosphate dehydrogenases
Author(s) -
Aziz Alaa,
JohnsonWinters Kayunta
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.01590
Subject(s) - cofactor , dehydrogenase , biochemistry , enzyme , chemistry , substrate (aquarium) , substrate specificity , biology , ecology
Our research has focused on F420‐dependent glucose‐6‐phosphate dehydrogenase (FGD), which is found within Mycobacteria. FGD catalyzes the conversion of glucose‐6‐ phosphate (G6P) to 6‐phosphogluconolactone, using oxidized F420 cofactor, which becomes reduced during catalysis. Our kinetic studies on FGD has led to important mechanistic insights to enzymes that utilize this lesser known cofactor. However, FGD from Mycobacteria only uses G6P as a substrate. Recently, a study has described new F 420‐dependent dehydrogenases which have a broader specificity of sugar substrates, known as FSDs [1]. FGD from Nocardioidaceae bacterium (FGD‐Noca) and FGD from Cryptosporangium arvum (FGD‐Cryar) are the two new sequences selected for these experimental determinations. The initial goals of this project are to express and purify FSDs and characterize the hydride transfer reaction mechanism using steady‐state and pre steady‐state kinetic methods. Our proposed experiments and preliminary results will be described here. Reference: M. Laura Mascotti, Hemant Kumar, Quoc‐Thai Nguyen, Maximiliano Juri Ayub, and Marco W. Fraaije. Reconstructing the evolutionary history of F420‐dependent dehydrogenases. Sci Report. 2018, 8: 17571.