Phosphogluconate dehydrogenase
Phosphogluconate dehydrogenase (also known as 6-phosphogluconate dehydrogenase or 6PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, a metabolic pathway parallel to glycolysis. This enzyme catalyzes the oxidative decarboxylation of 6-phosphogluconate into ribulose 5-phosphate in the presence of nicotinamide adenine dinucleotide phosphate (NADP+).
Function[edit | edit source]
The primary function of phosphogluconate dehydrogenase is to catalyze the conversion of 6-phosphogluconate, a six-carbon sugar, into ribulose 5-phosphate, a five-carbon sugar. This reaction also produces a molecule of NADPH, a crucial coenzyme in various biochemical reactions.
Structure[edit | edit source]
Phosphogluconate dehydrogenase is a dimeric enzyme, meaning it consists of two identical subunits. Each subunit contains a Rossmann fold domain for binding NADP+ and a substrate-binding domain.
Clinical significance[edit | edit source]
Alterations in the activity of phosphogluconate dehydrogenase have been associated with various diseases, including cancer and diabetes. In particular, increased activity of this enzyme has been observed in cancer cells, suggesting it may play a role in tumor growth and survival.
See also[edit | edit source]
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Contributors: Prab R. Tumpati, MD
