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Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity.

Proceedings of the National Academy of Sciences of the United States of America - 19 Jul 2022

Wei Xuepeng, Kixmoeller Kathryn, Baltrusaitis Elana, Yang Xiaolu, Marmorstein Ronen

Abstract excerpt

Human glucose-6-phosphate dehydrogenase (G6PD) is the main cellular source of NADPH, and thus plays a key role in maintaining reduced glutathione to protect cells from oxidative stress disorders such as hemolytic anemia. G6PD is a multimeric enzyme that uses the cofactors β-D-glucose 6-phosphate (G6P) and "catalytic" NADP+ (NADP+c), as well as a "structural" NADP+ (NADP+s) located ∼25 Å from the active site, to...

Topics

Catalytic Domain
Cryoelectron Microscopy
Glucosephosphate Dehydrogenase
Glucosephosphate Dehydrogenase Deficiency
Humans
Mutation
NADP
Protein Multimerization

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 35858355
DOI: 10.1073/pnas.2119695119
PMCID: PMC9303983

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