Details

Autor(en) / Beteiligte

• Davis, Lindsay A.
• Oyugi, Mercy A.
• Howard, Jamariya
• Corrales, Juan
• Aziz, Alaa
• Mandimutsira, Charlene
• Girme, Joisha
• Agbonoga, Amina
• Bashiri, Ghader
• Baker, Edward N.
• Johnson-Winters, Kayunta

Titel

F420-dependent glucose-6-phosphate dehydrogenase: A comprehensive review

Ist Teil von

• Inorganica Chimica Acta, 2021-09, Vol.524, p.120417, Article 120417

Ort / Verlag

Amsterdam: Elsevier B.V

Erscheinungsjahr

2021

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• [Display omitted] •The FGD catalyzed reaction is essential for the activation of a novel anti-TB drug compound and supplying reduced cofactor within M. tuberculosis.•Structural characterization of FGD has led to a proposed mechanism, which has been investigated using kinetic methods and updated.•Phylogenetic profiling has revealed additional FGDs in other microorganisms that utilize a variety of sugar-6-phosphates known as FSDs.•Structural and sequence comparison of FGD and G6PD has determined that while the two enzymes catalyze the same reaction, they are not of the same family of enzymes. F420-dependent glucose-6-phosphate dehydrogenase (FGD1) catalyzes the conversion of glucose-6-phosphate (G6P) to 6-phosphogluconolactone. During the course of this reaction, the oxidized cofactor F420 is converted to its reduced form (F420H2). FGD was initially identified and studied extensively within mycobacteria prior to the more recent discovery of FGDs from Rhodococcus jostii RHA1. Another group of FGDs that utilize a variety of sugar-6-phosphates from Nocardia and Cryptosporangium arvum is also known as the FSDs. Crystal structures of FGD from the pathogens Mycobacterium tuberculosis and Rhodococcus jostii RHA1 have provided significant insight into the structural and mechanistic properties of the enzymes and have been the basis for mutagenesis, kinetic and mechanistic studies in recent years. This review discusses the role of FGD within M. tuberculosis, followed by our current understanding of the FGD catalytic mechanism. This will also be discussed with reference to the relationship between FGD and the structurally unrelated NADP+-dependent glucose-6-phosphate enzymes.