Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme that is present in every single cell. It is responsible for catalyzing the first reaction of the pentose phosphate pathway where glucose-6-phosphate is oxidized to 6-phosphogluconolactone.
During this reaction, nicotinamide adenine dinucleotide phosphate (NADPH) is produced and it is responsible for multiple reductive biosynthetic reactions such as the regeneration of the reduced form of glutathione (GSH). Glutathione peroxidase in erythrocytes uses GSH to detoxify hydrogen peroxide by converting it to water. This important process is heavily reliant on the production of NADPH from the pentose phosphate pathway. Without NADPH, oxidized glutathione cannot be reduced to GSH which is required in the detoxification of hydrogen peroxide.
Therefore, G6PD deficiency in these cells will result in the decreased production of NADPH as this is the only NADPH-producing reaction which will lead to lower amounts of GSH in red blood cells. As red blood cells are highly sensitive to oxidative damage, they will be destroyed as they will not be able to detoxify hydrogen peroxide.
During this reaction, nicotinamide adenine dinucleotide phosphate (NADPH) is produced and it is responsible for multiple reductive biosynthetic reactions such as the regeneration of the reduced form of glutathione (GSH). Glutathione peroxidase in erythrocytes uses GSH to detoxify hydrogen peroxide by converting it to water. This important process is heavily reliant on the production of NADPH from the pentose phosphate pathway. Without NADPH, oxidized glutathione cannot be reduced to GSH which is required in the detoxification of hydrogen peroxide.
Therefore, G6PD deficiency in these cells will result in the decreased production of NADPH as this is the only NADPH-producing reaction which will lead to lower amounts of GSH in red blood cells. As red blood cells are highly sensitive to oxidative damage, they will be destroyed as they will not be able to detoxify hydrogen peroxide.